Dancing with Trojan horses: an interplay between the extracellular vesicles and viruses

References

• Affolabi, D., Torrea, G., Odoun, M., Senou, N., Ali Ligali, M., Anagonou, S., & Van Deun, A. (2010). Comparison of two LED fluorescence microscopy build-on modules for acid-fast smear microscopy. The International Journal of Tuberculosis and Lung Disease, 14(2), 160–164.
   PubMed Web of Science ®Google Scholar
• Aga, M., Bentz, G. L., Raffa, S., Torrisi, M. R., Kondo, S., Wakisaka, N., Yoshizaki, T., Pagano, J. S., & Shackelford, J. (2014). Exosomal HIF1alpha supports invasive potential of nasopharyngeal carcinoma-associated LMP1-positive exosomes. Oncogene, 33(37), 4613–4622. https://doi.org/10.1038/onc.2014.66
   PubMed Web of Science ®Google Scholar
• Ahmed, W., & Khan, G. (2014). The labyrinth of interactions of Epstein-Barr virus-encoded small RNAs. Reviews in Medical Virology, 24(1), 3–14. https://doi.org/10.1002/rmv.1763
   PubMed Web of Science ®Google Scholar
• Ahmed, W., Philip, P. S., Tariq, S., & Khan, G. (2014). Epstein-Barr virus-encoded small RNAs (EBERs) are present in fractions related to exosomes released by EBV-transformed cells. PloS One, 9(6), e99163. https://doi.org/10.1371/journal.pone.0099163
   PubMed Web of Science ®Google Scholar
• Akers, J. C., Gonda, D., Kim, R., Carter, B. S., & Chen, C. C. (2013). Biogenesis of extracellular vesicles (EV): Exosomes, microvesicles, retrovirus-like vesicles, and apoptotic bodies. Journal of Neuro-Oncology, 113(1), 1–11. https://doi.org/10.1007/s11060-013-1084-8
   PubMed Web of Science ®Google Scholar
• Alenquer, M., & Amorim, M. (2015). Exosome biogenesis, regulation, and function in viral infection. Viruses, 7(9), 5066–5083. https://doi.org/10.3390/v7092862
   PubMed Web of Science ®Google Scholar
• Altan-Bonnet, N. (2016). Extracellular vesicles are the Trojan horses of viral infection. Current Opinion in Microbiology., 32, 77–81. https://doi.org/10.1016/j.mib.2016.05.004
   PubMed Web of Science ®Google Scholar
• Andaloussi, S. E., Mäger, I., Breakefield, X. O., & Wood, M. J. (2013). Extracellular vesicles: Biology and emerging therapeutic opportunities. Nature Reviews Drug Discovery, 12(5), 347–357. https://doi.org/10.1038/nrd3978
   PubMed Web of Science ®Google Scholar
• Anderson, M. R., Kashanchi, F., & Jacobson, S. (2016). Exosomes in viral disease. Neurotherapeutics, 13(3), 535–546. https://doi.org/10.1007/s13311-016-0450-6
   PubMed Web of Science ®Google Scholar
• Andreu, Z., & Yáñez-Mó, M. (2014). Tetraspanins in extracellular vesicle formation and function. Frontiers in Immunology, 5, 442. https://doi.org/10.3389/fimmu.2014.00442
   PubMed Web of Science ®Google Scholar
• Antinori, A., Arendt, G., Becker, J. T., Brew, B. J., Byrd, D. A., Cherner, M., Clifford, D. B., Cinque, P., Epstein, L. G., Goodkin, K., Gisslen, M., Grant, I., Heaton, R. K., Joseph, J., Marder, K., Marra, C. M., McArthur, J. C., Nunn, M., Price, R. W., … Wojna, V. E. (2007). Updated research nosology for HIV-associated neurocognitive disorders. Neurology, 69(18), 1789–1799. https://doi.org/10.1212/01.WNL.0000287431.88658.8b
   PubMed Web of Science ®Google Scholar
• Arraud, N., Gounou, C., Linares, R., & Brisson, A. (2015). A simple flow cytometry method improves the detection of phosphatidylserine‐exposing extracellular vesicles. Journal of Thrombosis and Haemostasis, 13(2), 237–247. https://doi.org/10.1111/jth.12767
   PubMed Web of Science ®Google Scholar
• Arraud, N., Linares, R., Tan, S., Gounou, C., Pasquet, J. M., Mornet, S., & Brisson, A. R. (2014). Extracellular vesicles from blood plasma: Determination of their morphology, size, phenotype and concentration. Journal of Thrombosis and Haemostasis, 12(5), 614–627. https://doi.org/10.1111/jth.12554
   PubMed Web of Science ®Google Scholar
• Ashcroft, B., De Sonneville, J., Yuana, Y., Osanto, S., Bertina, R., Kuil, M., & Oosterkamp, T. (2012). Determination of the size distribution of blood microparticles directly in plasma using atomic force microscopy and microfluidics. Biomedical Microdevices, 14(4), 641–649. https://doi.org/10.1007/s10544-012-9642-y
   PubMed Web of Science ®Google Scholar
• Babuke, T., & Tikkanen, R. (2007). Dissecting the molecular function of reggie/flotillin proteins. European Journal of Cell Biology., 86(9), 525–532. https://doi.org/10.1016/j.ejcb.2007.03.003
   PubMed Web of Science ®Google Scholar
• Baietti, M. F., Zhang, Z., Mortier, E., Melchior, A., Degeest, G., Geeraerts, A., Ivarsson, Y., Depoortere, F., Coomans, C., Vermeiren, E., Zimmermann, P., & David, G. (2012). Syndecan-syntenin-ALIX regulates the biogenesis of exosomes. Nature Cell Biology, 14(7), 677–685. https://doi.org/10.1038/ncb2502
   PubMed Web of Science ®Google Scholar
• Barreto, A., Rodriguez, L. S., Rojas, O. L., Wolf, M., Greenberg, H. B., Franco, M. A., & Angel, J. (2010). Membrane vesicles released by intestinal epithelial cells infected with rotavirus inhibit T-cell function. Viral Immunology, 23(6), 595–608. https://doi.org/10.1089/vim.2009.0113
   PubMed Web of Science ®Google Scholar
• Bartel, D. P. (2004). MicroRNAs: Genomics, biogenesis, mechanism, and function. Cell, 116(2), 281–297. https://doi.org/10.1016/S0092-8674(04)00045-5
   PubMed Web of Science ®Google Scholar
• Batrakova, E. V., & Kim, M. S. (2015). Using exosomes, naturally-equipped nanocarriers, for drug delivery. Journal of Controlled Release, 219, 396–405. https://doi.org/10.1016/j.jconrel.2015.07.030
   PubMed Web of Science ®Google Scholar
• Baumgärtel, V., Ivanchenko, S., Dupont, A., Sergeev, M., Wiseman, P. W., Kräusslich, H.-G., Bräuchle, C., Müller, B., & Lamb, D. C. (2011). Live-cell visualization of dynamics of HIV budding site interactions with an ESCRT component. Nature Cell Biology, 13(4), 469–474. https://doi.org/10.1038/ncb2215
   PubMed Web of Science ®Google Scholar
• Bautista, D., Rodriguez, L. S., Franco, M. A., Angel, J., & Barreto, A. (2015). Caco-2 cells infected with rotavirus release extracellular vesicles that express markers of apoptotic bodies and exosomes. Cell Stress and Chaperones, 20(4), 697–708. https://doi.org/10.1007/s12192-015-0597-9
   PubMed Web of Science ®Google Scholar
• Bellingham, S. A., Coleman, B. M., & Hill, A. F. (2012). Small RNA deep sequencing reveals a distinct miRNA signature released in exosomes from prion-infected neuronal cells. Nucleic Acids Research, 40(21), 10937–10949. https://doi.org/10.1093/nar/gks832
   PubMed Web of Science ®Google Scholar
• Berditchevski, F., Odintsova, E., Sawada, S., & Gilbert, E. (2002). Expression of the palmitoylation-deficient CD151 weakens the association of alpha 3 beta 1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signaling. Journal of Biological Chemistry, 277(40), 36991–37000. https://doi.org/10.1074/jbc.M205265200
   PubMed Web of Science ®Google Scholar
• Bernard, H. U., Burk, R. D., Chen, Z., van Doorslaer, K., Hausen, H., & de Villiers, E. M. (2010). Classification of papillomaviruses (PVs) based on 189 PV types and proposal of taxonomic amendments. Virology, 401(1), 70–79. https://doi.org/10.1016/j.virol.2010.02.002
   PubMed Web of Science ®Google Scholar
• Betzig, E., Patterson, G. H., Sougrat, R., Lindwasser, O. W., Olenych, S., Bonifacino, J. S., Davidson, M. W., Lippincott-Schwartz, J., & Hess, H. F. (2006). Imaging intracellular fluorescent proteins at nanometer resolution. Science, 313(5793), 1642–1645. https://doi.org/10.1126/science.1127344
   PubMed Web of Science ®Google Scholar
• Bharat, T. A. M., Noda, T., Riches, J. D., Kraehling, V., Kolesnikova, L., Becker, S., Kawaoka, Y., & Briggs, J. A. G. (2012). Structural dissection of Ebola virus and its assembly determinants using cryo-electron tomography. Proceedings of the National Academy of Sciences, 109(11), 4275–4280. https://doi.org/10.1073/pnas.1120453109
   PubMed Web of Science ®Google Scholar
• Bhatnagar, S., & Schorey, J. S. (2007). Exosomes released from infected macrophages contain Mycobacterium avium glycopeptidolipids and are proinflammatory. Journal of Biological Chemistry, 282(35), 25779–25789. https://doi.org/10.1074/jbc.M702277200
   PubMed Web of Science ®Google Scholar
• Bhatnagar, S., Shinagawa, K., Castellino, F. J., & Schorey, J. S. (2007). Exosomes released from macrophages infected with intracellular pathogens stimulate a proinflammatory response in vitro and in vivo. Blood, 110(9), 3234–3244. https://doi.org/10.1182/blood-2007-03-079152
   PubMed Web of Science ®Google Scholar
• Bhatt, S., Gething, P. W., Brady, O. J., Messina, J. P., Farlow, A. W., Moyes, C. L., Drake, J. M., Brownstein, J. S., Hoen, A. G., Sankoh, O., Myers, M. F., George, D. B., Jaenisch, T., Wint, G. R. W., Simmons, C. P., Scott, T. W., Farrar, J. J., & Hay, S. I. (2013). The global distribution and burden of dengue. Nature, 496(7446), 504–507. https://doi.org/10.1038/nature12060
   PubMed Web of Science ®Google Scholar
• Bickel, P. E., Scherer, P. E., Schnitzer, J. E., Oh, P., Lisanti, M. P., & Lodish, H. F. (1997). Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins. Journal of Biological Chemistry, 272(21), 13793–13802. https://doi.org/10.1074/jbc.272.21.13793
   PubMed Web of Science ®Google Scholar
• Bird, S. W., Maynard, N. D., Covert, M. W., & Kirkegaard, K. (2014). Nonlytic viral spread enhanced by autophagy components. Proceedings of the National Academy of Sciences, 111(36), 13081–13086. https://doi.org/10.1073/pnas.1401437111
   PubMed Web of Science ®Google Scholar
• Bissig, C., & Gruenberg, J. (2014). ALIX and the multivesicular endosome: ALIX in Wonderland. Trends in Cell Biology., 24(1), 19–25. https://doi.org/10.1016/j.tcb.2013.10.009
   PubMed Web of Science ®Google Scholar
• Bobrie, A., Colombo, M., Raposo, G., & Théry, C. (2011). Exosome secretion: Molecular mechanisms and roles in immune responses. Traffic, 12(12), 1659–1668. https://doi.org/10.1111/j.1600-0854.2011.01225.x
   PubMed Web of Science ®Google Scholar
• Bodin, S., Planchon, D., Rios Morris, E., Comunale, F., & Gauthier-Rouviere, C. (2014). Flotillins in intercellular adhesion - From cellular physiology to human diseases. Journal of Cell Science., 127(24), 5139–5147. https://doi.org/10.1242/jcs.159764
   PubMed Web of Science ®Google Scholar
• Braicu, C., Tomuleasa, C., Monroig, P., Cucuianu, A., Berindan-Neagoe, I., & Calin, G. (2015). Exosomes as divine messengers: Are they the Hermes of modern molecular oncology? Cell Death & Differentiation, 22(1), 34–45. https://doi.org/10.1038/cdd.2014.130
   PubMed Web of Science ®Google Scholar
• Brass, A. L., Huang, I.-C., Benita, Y., John, S. P., Krishnan, M. N., Feeley, E. M., Ryan, B. J., Weyer, J. L., van der Weyden, L., Fikrig, E., Adams, D. J., Xavier, R. J., Farzan, M., & Elledge, S. J. (2009). The IFITM proteins mediate cellular resistance to influenza A H1N1 virus, West Nile virus, and dengue virus. Cell, 139(7), 1243–1254. https://doi.org/10.1016/j.cell.2009.12.017
   PubMed Web of Science ®Google Scholar
• Bukong, T. N., Momen-Heravi, F., Kodys, K., Bala, S., & Szabo, G. (2014). Exosomes from hepatitis C infected patients transmit HCV infection and contain replication competent viral RNA in complex with Ago2-miR122-HSP90. PLoS Pathogens, 10(10), e1004424. https://doi.org/10.1371/journal.ppat.1004424
   PubMed Web of Science ®Google Scholar
• Caby, M.-P., Lankar, D., Vincendeau-Scherrer, C., Raposo, G., & Bonnerot, C. (2005). Exosomal-like vesicles are present in human blood plasma. International Immunology, 17(7), 879–887. https://doi.org/10.1093/intimm/dxh267
   PubMed Web of Science ®Google Scholar
• Cai, S., Luo, B., Jiang, P., Zhou, X., Lan, F., Yi, Q., & Wu, Y. (2018). Immuno-modified superparamagnetic nanoparticles via host-guest interactions for high-purity capture and mild release of exosomes. Nanoscale, 10(29), 14280–14289. https://doi.org/10.1039/C8NR02871K
   PubMed Web of Science ®Google Scholar
• Calistri, A., Sette, P., Salata, C., Cancellotti, E., Forghieri, C., Comin, A., GöTtlinger, H., Campadelli-Fiume, G., Palù, G., & Parolin, C., (2007). Intracellular trafficking and maturation of herpes simplex virus type 1 gB and virus egress require functional biogenesis of multivesicular bodies. Journal of Virology, 81(20), 11468–11478. https://doi.org/10.1128/JVI.01364-07
   PubMed Web of Science ®Google Scholar
• Campadelli-Fiume, G., Mirandola, P., & Menotti, L. (1999). Human herpesvirus 6: An emerging pathogen. Emerging Infectious Diseases, 5(3), 353–366. https://doi.org/10.3201/eid0503.990306
   PubMed Web of Science ®Google Scholar
• Campbell, T. D., Khan, M., Huang, M. B., Bond, V. C., & Powell, M. D. (2008). HIV-1 Nef protein is secreted into vesicles that can fuse with target cells and virions. Ethn Dis, 18(2 Suppl 2), 14–19.
   Google Scholar
• Campen, A., Williams, R. M., Brown, C. J., Meng, J., Uversky, V. N., & Dunker, A. K. (2008). TOP-IDP-scale: A new amino acid scale measuring propensity for intrinsic disorder. Protein & Peptide Letters, 15(9), 956–963. https://doi.org/10.2174/092986608785849164
   PubMed Web of Science ®Google Scholar
• Canitano, A., Venturi, G., Borghi, M., Ammendolia, M. G., & Fais, S. (2013). Exosomes released in vitro from Epstein-Barr virus (EBV)-infected cells contain EBV-encoded latent phase mRNAs. Cancer Letters, 337(2), 193–199. https://doi.org/10.1016/j.canlet.2013.05.012
   PubMed Web of Science ®Google Scholar
• Carlton, J. G., Agromayor, M., & Martin-Serrano, J. (2008). Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release. Proceedings of the National Academy of Sciences, 105(30), 10541–10546. https://doi.org/10.1073/pnas.0802008105
   PubMed Web of Science ®Google Scholar
• Carlton, J. G., & Martin-Serrano, J. (2007). Parallels between cytokinesis and retroviral budding: A role for the ESCRT machinery. Science, 316(5833), 1908–1912. https://doi.org/10.1126/science.1143422
   PubMed Web of Science ®Google Scholar
• Caserta, M. T., & Hall, C. B. (1993). Human herpesvirus-6. Annual Review of Medicine, 44(1), 377–383. https://doi.org/10.1146/annurev.me.44.020193.002113
   PubMedGoogle Scholar
• Chahar, H. S., Bao, X., & Casola, A. (2015). Exosomes and their role in the life cycle and pathogenesis of RNA viruses. Viruses, 7(6), 3204–3225. https://doi.org/10.3390/v7062770
   PubMed Web of Science ®Google Scholar
• Chahar, H. S., Corsello, T., Kudlicki, A. S., Komaravelli, N., & Casola, A. (2018). Respiratory syncytial virus infection changes cargo composition of exosome released from airway epithelial cells. Scientific Reports, 8(1), 387. https://doi.org/10.1038/s41598-017-18672-5
   PubMed Web of Science ®Google Scholar
• Chan, Y. K., Huang, I.-C., & Farzan, M. (2012). IFITM proteins restrict antibody-dependent enhancement of dengue virus infection. PloS One, 7(3), e34508. https://doi.org/10.1371/journal.pone.0034508
   PubMed Web of Science ®Google Scholar
• Chayavichitsilp, P., Buckwalter, J. V., Krakowski, A. C., & Friedlander, S. F. (2009). Herpes simplex. Pediatrics in Review, 30(4), 119–130. https://doi.org/10.1542/pir.30-4-119
   PubMed Web of Science ®Google Scholar
• Chen, H., Liu, X., Li, Z., Zhan, P., & De Clercq, E. (2010). TSG101: A novel anti-HIV-1 drug target. Current Medicinal Chemistry, 17(8), 750–758. https://doi.org/10.2174/092986710790514444
   PubMed Web of Science ®Google Scholar
• Chen, Y.-H., Du, WLi., Hagemeijer, M. C., Takvorian, P. M., Pau, C., Cali, A., Brantner, C. A., Stempinski, E. S., Connelly, P. S., Ma, H.-C., Jiang, P., Wimmer, E., Altan-Bonnet, G., & Altan-Bonnet, N. (2015). Phosphatidylserine vesicles enable efficient en bloc transmission of enteroviruses. Cell, 160(4), 619–630. https://doi.org/10.1016/j.cell.2015.01.032
   PubMed Web of Science ®Google Scholar
• Cheng, L., Sharples, R. A., Scicluna, B. J., & Hill, A. F. (2014). Exosomes provide a protective and enriched source of miRNA for biomarker profiling compared to intracellular and cell-free blood. Journal of Extracellular Vesicles, 3(1), 23743. https://doi.org/10.3402/jev.v3.23743
   PubMedGoogle Scholar
• Cheng, Y., Oldfield, C. J., Meng, J., Romero, P., Uversky, V. N., & Dunker, A. K. (2007). Mining alpha-helix-forming molecular recognition features with cross species sequence alignments. Biochemistry, 46(47), 13468–13477. https://doi.org/10.1021/bi7012273
   PubMed Web of Science ®Google Scholar
• Chugh, P. E., Sin, S.-H., Ozgur, S., Henry, D. H., Menezes, P., Griffith, J., Eron, J. J., Damania, B., & Dittmer, D. P. (2013). Systemically circulating viral and tumor-derived microRNAs in KSHV-associated malignancies. PLoS Pathogens, 9(7), e1003484. https://doi.org/10.1371/journal.ppat.1003484
   PubMed Web of Science ®Google Scholar
• Chung, H.-Y., Morita, E., von Schwedler, U., MüLler, B., KräUsslich, H.-G., & Sundquist, W. I., (2008). NEDD4L overexpression rescues the release and infectivity of human immunodeficiency virus type 1 constructs lacking PTAP and YPXL late domains. Journal of Virology, 82(10), 4884–4897. https://doi.org/10.1128/JVI.02667-07
   PubMed Web of Science ®Google Scholar
• Citkowicz, A., Petry, H., Harkins, R. N., Ast, O., Cashion, L., Goldmann, C., Bringmann, P., Plummer, K., & Larsen, B. R. (2008). Characterization of virus-like particle assembly for DNA delivery using asymmetrical flow field-flow fractionation and light scattering. Analytical Biochemistry, 376(2), 163–172. https://doi.org/10.1016/j.ab.2008.02.011
   PubMed Web of Science ®Google Scholar
• Clague, M. J., Liu, H., & Urbe, S. (2012). Governance of endocytic trafficking and signaling by reversible ubiquitylation. Developmental Cell, 23(3), 457–467. https://doi.org/10.1016/j.devcel.2012.08.011
   PubMed Web of Science ®Google Scholar
• Clayton, A., Court, J., Navabi, H., Adams, M., Mason, M. D., Hobot, J. A., Newman, G. R., & Jasani, B. (2001). Analysis of antigen presenting cell derived exosomes, based on immuno-magnetic isolation and flow cytometry. Journal of Immunological Methods, 247(1–2), 163–174. https://doi.org/10.1016/S0022-1759(00)00321-5
   PubMed Web of Science ®Google Scholar
• Coelho Ribeiro, M. d L., Espinosa, J., Islam, S., Martinez, O., Thanki, J. J., Mazariegos, S., Nguyen, T., Larina, M., Xue, B., & Uversky, V. N. (2013). Malleable ribonucleoprotein machine: Protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome. Peer Journal, 1, e2. https://doi.org/10.7717/peerj.2
   PubMed Web of Science ®Google Scholar
• Coleman, B. M., Hanssen, E., Lawson, V. A., & Hill, A. F. (2012). Prion-infected cells regulate the release of exosomes with distinct ultrastructural features. The FASEB Journal, 26(10), 4160–4173. https://doi.org/10.1096/fj.11-202077
   PubMed Web of Science ®Google Scholar
• Crump, C. M., Yates, C., & Minson, T. (2007). Herpes simplex virus type 1 cytoplasmic envelopment requires functional Vps4. Journal of Virology, 81(14), 7380–7387. https://doi.org/10.1128/JVI.00222-07
   PubMed Web of Science ®Google Scholar
• Cysique, L. A., Maruff, P., & Brew, B. J. (2004). Prevalence and pattern of neuropsychological impairment in human immunodeficiency virus-infected/acquired immunodeficiency syndrome (HIV/AIDS) patients across pre- and post-highly active antiretroviral therapy eras: A combined study of two cohorts. Journal of Neurovirology, 10(6), 350–357. https://doi.org/10.1080/13550280490521078
   PubMed Web of Science ®Google Scholar
• Damania, B. (2007). DNA tumor viruses and human cancer. Trends in Microbiology., 15(1), 38–44. https://doi.org/10.1016/j.tim.2006.11.002
   PubMed Web of Science ®Google Scholar
• Darling, A. L., & Uversky, V. N. (2017). Intrinsic disorder in proteins with pathogenic repeat expansions. Molecules, 22(12), 2027. https://doi.org/10.3390/molecules22122027
   PubMed Web of Science ®Google Scholar
• Daughdrill, G. W., Pielak, G. J., Uversky, V. N., Cortese, M. S., & Dunker, A. K. (2005). Natively disordered proteins. In J. Buchner & T. Kiefhaber (Eds.), Handbook of protein folding (pp. 271–353). Wiley-VCH, Verlag GmbH & Co. KGaA.
   Google Scholar
• Davies, R. T., Kim, J., Jang, S. C., Choi, E. J., Gho, Y. S., & Park, J. (2012). Microfluidic filtration system to isolate extracellular vesicles from blood. Lab on a Chip, 12(24), 5202–5210. https://doi.org/10.1039/c2lc41006k
   PubMed Web of Science ®Google Scholar
• de Gassart, A., Géminard, C., Février, B., Raposo, Ga., & Vidal, Michel., (2003). Lipid raft-associated protein sorting in exosomes. Blood, 102(13), 4336–4344. https://doi.org/10.1182/blood-2003-03-0871
   PubMed Web of Science ®Google Scholar
• de The, G., & Kazanji, M. (1996). An HTLV-I/II vaccine: From animal models to clinical trials? Journal of Acquired Immune Deficiency Syndromes and Human Retrovirology, 13 (Suppl 1), S191–S198.
   PubMedGoogle Scholar
• de Villiers, E. M., Fauquet, C., Broker, T. R., Bernard, H. U., & Zur Hausen, H. (2004). Classification of papillomaviruses. Virology, 324(1), 17–27. https://doi.org/10.1016/j.virol.2004.03.033
   PubMed Web of Science ®Google Scholar
• DeForte, S., & Uversky, V. N. (2016). Order, disorder, and everything in between. Molecules, 21(8), 1090. https://doi.org/10.3390/molecules21081090
   Web of Science ®Google Scholar
• DeForte, S., & Uversky, V. N. (2017). Not an exception to the rule: The functional significance of intrinsically disordered protein regions in enzymes. Molecular Biosystems, 13(3), 463–469. https://doi.org/10.1039/C6MB00741D
   PubMedGoogle Scholar
• Demirov, D. G., Ono, A., Orenstein, J. M., & Freed, E. O. (2002). Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function. Proceedings of the National Academy of Sciences, 99(2), 955–960. https://doi.org/10.1073/pnas.032511899
   PubMed Web of Science ®Google Scholar
• Der, S. D., Zhou, A., Williams, B. R., & Silverman, R. H. (1998). Identification of genes differentially regulated by interferon alpha, beta, or gamma using oligonucleotide arrays. Proceedings of the National Academy of Sciences, 95(26), 15623–15628. https://doi.org/10.1073/pnas.95.26.15623
   PubMed Web of Science ®Google Scholar
• Dermine, J. F., Duclos, S., Garin, J., St-Louis, F., Rea, S., Parton, R. G., & Desjardins, M. (2001). Flotillin-1-enriched lipid raft domains accumulate on maturing phagosomes. Journal of Biological Chemistry, 276(21), 18507–18512. https://doi.org/10.1074/jbc.M101113200
   PubMed Web of Science ®Google Scholar
• Devhare, P. B., Sasaki, R., Shrivastava, S., Di Bisceglie, A. M., Ray, R., & Ray, R. B. (2017). Exosome-mediated intercellular communication between hepatitis C virus-infected hepatocytes and hepatic stellate cells. Journal of Virology, 91(6), e02225. https://doi.org/10.1128/JVI.02225-16
   PubMed Web of Science ®Google Scholar
• Di Domenico, T., Walsh, I., & Tosatto, S. C. (2013). Analysis and consensus of currently available intrinsic protein disorder annotation sources in the MobiDB database. BMC Bioinformatics, 14 (Suppl 7), S3. https://doi.org/10.1186/1471-2105-14-S7-S3
   PubMedGoogle Scholar
• Diamond, M. S., & Pierson, T. C. (2015). Molecular insight into dengue virus pathogenesis and its implications for disease control. Cell, 162(3), 488–492. https://doi.org/10.1016/j.cell.2015.07.005
   PubMed Web of Science ®Google Scholar
• Dias, M. V. S., Costa, C. S., & daSilva, L. L. P. (2018). The ambiguous roles of extracellular vesicles in HIV replication and pathogenesis Frontiers in Microbiology, 9, 2411. https://doi.org/10.3389/fmicb.2018.02411
   PubMed Web of Science ®Google Scholar
• Djulbegovic, M. B., & Uversky, V. N. (2019). Ferroptosis: An iron- and disorder-dependent programmed cell death. International Journal of Biological Macromolecules., 135, 1052–1069. https://doi.org/10.1016/j.ijbiomac.2019.05.221
   PubMed Web of Science ®Google Scholar
• Doniger, J., Muralidhar, S., & Rosenthal, L. J. (1999). Human cytomegalovirus and human herpesvirus 6 genes that transform and transactivate. Clinical Microbiology Reviews, 12(3), 367–382. https://doi.org/10.1128/CMR.12.3.367
   PubMed Web of Science ®Google Scholar
• Dores, M. R., Chen, B., Lin, H., Soh, U. J. K., Paing, M. M., Montagne, W. A., Meerloo, T., & Trejo, J. A. (2012). ALIX binds a YPX(3)L motif of the GPCR PAR1 and mediates ubiquitin-independent ESCRT-III/MVB sorting. The Journal of Cell Biology, 197(3), 407–419. https://doi.org/10.1083/jcb.201110031
   PubMed Web of Science ®Google Scholar
• Dores, M. R., Paing, M. M., Lin, H., Montagne, W. A., Marchese, A., & Trejo, J. (2012). AP-3 regulates PAR1 ubiquitin-independent MVB/lysosomal sorting via an ALIX-mediated pathway. Molecular Biology of the Cell, 23(18), 3612–3623. https://doi.org/10.1091/mbc.e12-03-0251
   PubMed Web of Science ®Google Scholar
• Dosztanyi, Z., Csizmok, V., Tompa, P., & Simon, I. (2005). IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics, 21(16), 3433–3434. https://doi.org/10.1093/bioinformatics/bti541
   PubMed Web of Science ®Google Scholar
• Douek, D. C., Roederer, M., & Koup, R. A. (2009). Emerging concepts in the immunopathogenesis of AIDS. Annual Review of Medicine, 60(1), 471–484. https://doi.org/10.1146/annurev.med.60.041807.123549
   PubMedGoogle Scholar
• Dowlatshahi, D. P., Sandrin, V., Vivona, S., Shaler, T. A., Kaiser, S. E., Melandri, F., Sundquist, W. I., & Kopito, R. R. (2012). ALIX is a Lys63-specific polyubiquitin binding protein that functions in retrovirus budding. Developmental Cell, 23(6), 1247–1254. https://doi.org/10.1016/j.devcel.2012.10.023
   PubMed Web of Science ®Google Scholar
• Dreux, M., Garaigorta, U., Boyd, B., Décembre, E., Chung, J., Whitten-Bauer, C., Wieland, S., & Chisari, F. V. (2012). Short-range exosomal transfer of viral RNA from infected cells to plasmacytoid dendritic cells triggers innate immunity. Cell Host & Microbe., 12(4), 558–570. https://doi.org/10.1016/j.chom.2012.08.010
   PubMed Web of Science ®Google Scholar
• Duffield, A., Kamsteeg, E. J., Brown, A. N., Pagel, P., & Caplan, M. J. (2003). The tetraspanin CD63 enhances the internalization of the H,K-ATPase beta-subunit. Proceedings of the National Academy of Sciences, 100(26), 15560–15565. https://doi.org/10.1073/pnas.2536699100
   PubMed Web of Science ®Google Scholar
• Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradovic, Z. (2002). Intrinsic disorder and protein function. Biochemistry, 41(21), 6573–6582.
   PubMed Web of Science ®Google Scholar
• Dunker, A. K., Brown, C. J., & Obradovic, Z. (2002). Identification and functions of usefully disordered proteins. Advances in Protein Chemistry, 62, 25–49. https://doi.org/10.1016/s0065-3233(02)62004-2
   PubMedGoogle Scholar
• Dunker, A. K., Garner, E., Guilliot, S., Romero, P., Albrecht, K., Hart, J., … Villafranca, J. E. (1998). Protein disorder and the evolution of molecular recognition: Theory, predictions and observations. Pacific Symposium on Biocomputing, 1998, 473–484.
   Google Scholar
• Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., Ausio, J., Nissen, M. S., Reeves, R., Kang, C. H., Kissinger, C. R., Bailey, R. W., Griswold, M. D., Chiu, W., Garner, E. C., & Obradovic, Z. (2001). Intrinsically disordered protein. Journal of Molecular Graphics and Modelling, 19(1), 26–59. https://doi.org/10.1016/S1093-3263(00)00138-8
   PubMed Web of Science ®Google Scholar
• Dunker, A. K., Obradovic, Z., Romero, P., Garner, E. C., & Brown, C. J. (2000). Intrinsic protein disorder in complete genomes. Genome Informatics: Workshop on Genome Informatics, 11, 161–171.
   PubMedGoogle Scholar
• Dyson, H. J. (2011). Expanding the proteome: Disordered and alternatively folded proteins. Quarterly Reviews of Biophysics, 44(4), 467–518. https://doi.org/10.1017/S0033583511000060
   PubMed Web of Science ®Google Scholar
• Eitan, E., Suire, C., Zhang, S., & Mattson, M. P. (2016). Impact of lysosome status on extracellular vesicle content and release. Ageing Research Reviews, 32, 65–74. https://doi.org/10.1016/j.arr.2016.05.001
   PubMed Web of Science ®Google Scholar
• Escola, J. M., Kleijmeer, M. J., Stoorvogel, W., Griffith, J. M., Yoshie, O., & Geuze, H. J. (1998). Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes. Journal of Biological Chemistry, 273(32), 20121–20127. https://doi.org/10.1074/jbc.273.32.20121
   PubMed Web of Science ®Google Scholar
• Everitt, A. R., Clare, S., Pertel, T., John, S. P., Wash, R. S., Smith, S. E., Chin, C. R., Feeley, E. M., Sims, J. S., Adams, D. J., Wise, H. M., Kane, L., Goulding, D., Digard, P., Anttila, V., Baillie, J. K., Walsh, T. S., …. Kellam, P. (2012). IFITM3 restricts the morbidity and mortality associated with influenza. Nature, 484(7395), 519–523. https://doi.org/10.1038/nature10921
   PubMed Web of Science ®Google Scholar
• Fader, C. M., & Colombo, M. I. (2009). Autophagy and multivesicular bodies: Two closely related partners. Cell Death & Differentiation, 16(1), 70–78. https://doi.org/10.1038/cdd.2008.168
   PubMed Web of Science ®Google Scholar
• Fang, Y., Wu, N., Gan, X., Yan, W., Morrell, J. C., & Gould, S. J. (2007). Higher-order oligomerization targets plasma membrane proteins and HIV gag to exosomes. PLoS Biology, 5(6), e158. https://doi.org/10.1371/journal.pbio.0050158
   PubMed Web of Science ®Google Scholar
• Feeley, E. M., Sims, J. S., John, S. P., Chin, C. R., Pertel, T., Chen, L.-M., Gaiha, G. D., Ryan, B. J., Donis, R. O., Elledge, S. J., & Brass, A. L. (2011). IFITM3 inhibits influenza A virus infection by preventing cytosolic entry. PLoS Pathogens, 7(10), e1002337. https://doi.org/10.1371/journal.ppat.1002337
   PubMed Web of Science ®Google Scholar
• Feng, S., Zeng, D., Zheng, J., & Zhao, D. (2018). MicroRNAs: Mediators and therapeutic targets to airway hyper reactivity after respiratory syncytial virus infection. Frontiers in Microbiology, 9, 2177. https://doi.org/10.3389/fmicb.2018.02177
   PubMed Web of Science ®Google Scholar
• Feng, Z., Hensley, L., McKnight, K. L., Hu, F., Madden, V., Ping, L. F., Jeong, S.-H., Walker, C., Lanford, R. E., & Lemon, S. M. (2013). A pathogenic picornavirus acquires an envelope by hijacking cellular membranes. Nature, 496(7445), 367–371. https://doi.org/10.1038/nature12029
   PubMed Web of Science ®Google Scholar
• Feng, Z., Li, Y., McKnight, K. L., Hensley, L., Lanford, R. E., Walker, C. M., & Lemon, S. M. (2015). Human pDCs preferentially sense enveloped hepatitis A virions. Journal of Clinical Investigation, 125(1), 169–176. https://doi.org/10.1172/JCI77527
   PubMed Web of Science ®Google Scholar
• Florin, L., & Lang, T. (2018). Tetraspanin assemblies in virus infection. Frontiers in Immunology, 9, 1140. https://doi.org/10.3389/fimmu.2018.01140
   PubMedGoogle Scholar
• Fonin, A. V., Darling, A. L., Kuznetsova, I. M., Turoverov, K. K., & Uversky, V. N. (2019). Multi-functionality of proteins involved in GPCR and G protein signaling: Making sense of structure-function continuum with intrinsic disorder-based proteoforms. Cellular and Molecular Life Sciences, 76, 4461–4492.
   PubMed Web of Science ®Google Scholar
• Freed, E. O. (2015). HIV-1 assembly, release and maturation. Nature Reviews Microbiology, 13(8), 484–496. https://doi.org/10.1038/nrmicro3490
   PubMed Web of Science ®Google Scholar
• Fuxreiter, M., Tóth-Petróczy, Á., Kraut, D. A., Matouschek, A. T., Lim, R. Y. H., Xue, B., Kurgan, L., & Uversky, V. N. (2014). Disordered proteinaceous machines. Chemical Reviews, 114(13), 6806–6843. https://doi.org/10.1021/cr4007329
   PubMed Web of Science ®Google Scholar
• Gaiffe, E., Prétet, J.-L., Launay, S., Jacquin, E., Saunier, M., Hetzel, G., Oudet, P., & Mougin, C. (2012). Apoptotic HPV positive cancer cells exhibit transforming properties. PloS One, 7(5), e36766. https://doi.org/10.1371/journal.pone.0036766
   PubMed Web of Science ®Google Scholar
• Gallegos-Orozco, J. F., & Rakela-Brodner, J. (2010). Hepatitis viruses: Not always what it seems to be. Revista medica de Chile, 138(10), 1302–1311.
   PubMed Web of Science ®Google Scholar
• Garner, E., Cannon, P., Romero, P., Obradovic, Z., & Dunker, A. K. (1998). Predicting disordered regions from amino acid sequence: Common themes despite differing structural characterization. Genome Informatics. Workshop on Genome Informatics, 9, 201–213.
   PubMedGoogle Scholar
• Garner, E., Romero, P., Dunker, A. K., Brown, C., & Obradovic, Z. (1999). Predicting binding regions within disordered proteins. Genome Informatics. Workshop on Genome Informatics, 10, 41–50.
   PubMedGoogle Scholar
• Garrus, J. E., von Schwedler, U. K., Pornillos, O. W., Morham, S. G., Zavitz, K. H., Wang, H. E., Wettstein, D. A., Stray, K. M., Côté, M., Rich, R. L., Myszka, D. G., & Sundquist, W. I. (2001). Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell, 107(1), 55–65. https://doi.org/10.1016/S0092-8674(01)00506-2
   PubMed Web of Science ®Google Scholar
• Gheinani, A. H., Vögeli, M., Baumgartner, U., Vassella, E., Draeger, A., Burkhard, F. C., & Monastyrskaya, K. (2018). Improved isolation strategies to increase the yield and purity of human urinary exosomes for biomarker discovery. Scientific Reports, 8(1), 3945. https://doi.org/10.1038/s41598-018-22142-x
   PubMedGoogle Scholar
• Giebel, B., & Helmbrecht, C. (2017). Methods to analyze EVs. In Exosomes and microvesicles (pp. 1–20). Springer.
   Google Scholar
• Giugliano, S., Kriss, M., Golden-Mason, L., Dobrinskikh, E., Stone, A. E. L., Soto-Gutierrez, A., Mitchell, A., Khetani, S. R., Yamane, D., Stoddard, M., Li, H., Shaw, G. M., Edwards, M. G., Lemon, S. M., Gale, M., Shah, V. H., & Rosen, H. R. (2015). Hepatitis C virus infection induces autocrine interferon signaling by human liver endothelial cells and release of exosomes, which inhibits viral replication. Gastroenterology, 148(2), 392–402. https://doi.org/10.1053/j.gastro.2014.10.040
   PubMed Web of Science ®Google Scholar
• Gonçalves, D. U., Proietti, F. A., Ribas, J. G. R., Araújo, M. G., Pinheiro, S. R., Guedes, A. C., & Carneiro-Proietti, A. B. F., (2010). Epidemiology, treatment, and prevention of human T-cell leukemia virus type 1-associated diseases. Clinical Microbiology Reviews, 23(3), 577–589. CMR, 00063-09 https://doi.org/10.1128/
   PubMed Web of Science ®Google Scholar
• Gould, S. J., Booth, A. M., & Hildreth, J. E. (2003). The Trojan exosome hypothesis. Proceedings of the National Academy of Sciences, 100(19), 10592–10597. https://doi.org/10.1073/pnas.1831413100
   PubMed Web of Science ®Google Scholar
• Griffiths-Jones, S. (2004). The microRNA registry. Nucleic Acids Research, 32(suppl_1), D109–D111.
   PubMedGoogle Scholar
• Griffiths, P. D., & Walter, S. (2005). Cytomegalovirus. Current Opinion in Infectious Diseases, 18(3), 241–245. https://doi.org/10.1097/01.qco.0000168385.39390.1b
   PubMed Web of Science ®Google Scholar
• Gruenberg, J. (2009). Viruses and endosome membrane dynamics. Current Opinion in Cell Biology., 21(4), 582–588. https://doi.org/10.1016/j.ceb.2009.03.008
   PubMed Web of Science ®Google Scholar
• Gruenberg, J., & van der Goot, F. G. (2006). Mechanisms of pathogen entry through the endosomal compartments. Nature Reviews Molecular Cell Biology, 7(7), 495–504. https://doi.org/10.1038/nrm1959
   PubMed Web of Science ®Google Scholar
• Guenat, D., Hermetet, F., Pretet, J. L., & Mougin, C. (2017). Exosomes and other extracellular vesicles in HPV transmission and carcinogenesis. Viruses, 9(8), 211. https://doi.org/10.3390/v9080211
   Web of Science ®Google Scholar
• Gutzeit, C., Nagy, N., Gentile, M., Lyberg, K., Gumz, J., Vallhov, H., Puga, I., Klein, E., Gabrielsson, S., Cerutti, A., & Scheynius, A. (2014). Exosomes derived from Burkitt’s lymphoma cell lines induce proliferation, differentiation, and class-switch recombination in B cells. The Journal of Immunology, 192(12), 5852–5862. https://doi.org/10.4049/jimmunol.1302068
   PubMed Web of Science ®Google Scholar
• Habchi, J., Tompa, P., Longhi, S., & Uversky, V. N. (2014). Introducing protein intrinsic disorder. Chemical Reviews, 114(13), 6561–6588. https://doi.org/10.1021/cr400514h
   PubMed Web of Science ®Google Scholar
• Han, Z., Liu, X., Chen, X., Zhou, X., Du, T., Roizman, B., & Zhou, G. (2016). miR-H28 and miR-H29 expressed late in productive infection are exported and restrict HSV-1 replication and spread in recipient cells. Proceedings of the National Academy of Sciences, 113(7), E894–901. https://doi.org/10.1073/pnas.1525674113
   PubMed Web of Science ®Google Scholar
• Harden, M. E., & Munger, K. (2017). Human papillomavirus 16 E6 and E7 oncoprotein expression alters microRNA expression in extracellular vesicles. Virology, 508, 63–69. https://doi.org/10.1016/j.virol.2017.05.005
   PubMed Web of Science ®Google Scholar
• Harding, C., Heuser, J., & Stahl, P. (1983). Receptor-mediated endocytosis of transferrin and recycling of the transferrin receptor in rat reticulocytes. The Journal of Cell Biology, 97(2), 329–339. https://doi.org/10.1083/jcb.97.2.329
   PubMed Web of Science ®Google Scholar
• Harding, C., Heuser, J., & Stahl, P. (1984). Endocytosis and intracellular processing of transferrin and colloidal gold-transferrin in rat reticulocytes: Demonstration of a pathway for receptor shedding. European Journal of Cell Biology, 35(2), 256–263.
   PubMed Web of Science ®Google Scholar
• Hauser, P., Wang, S., & Didenko, V. V. (2017). Apoptotic bodies: Selective detection in extracellular vesicles. Methods in Molecular Biology (Clifton, NJ), 1554, 193–200. https://doi.org/10.1007/978-1-4939-6759-9_12
   PubMedGoogle Scholar
• Heaton, R. K., Clifford, D. B., Franklin, D. R., Woods, S. P., Ake, C., Vaida, F., Ellis, R. J., Letendre, S. L., Marcotte, T. D., Atkinson, J. H., Rivera-Mindt, M., Vigil, O. R., Taylor, M. J., Collier, A. C., Marra, C. M., Gelman, B. B., McArthur, J. C., Morgello, S., Simpson, D. M., McCutchan, J. A., Abramson, I., … CHARTER Group. (2010). HIV-associated neurocognitive disorders persist in the era of potent antiretroviral therapy: CHARTER Study. Neurology, 75(23), 2087–2096. https://doi.org/10.1212/WNL.0b013e318200d727
   PubMed Web of Science ®Google Scholar
• Hegyi, H., & Tompa, P. (2012). Increased structural disorder of proteins encoded on human sex chromosomes. Molecular Biosystems., 8(1), 229–236. https://doi.org/10.1039/C1MB05285C
   PubMedGoogle Scholar
• Heinemann, M. L., Ilmer, M., Silva, L. P., Hawke, D. H., Recio, A., Vorontsova, M. A., Alt, E., & Vykoukal, J. (2014). Benchtop isolation and characterization of functional exosomes by sequential filtration. Journal of Chromatography A, 1371, 125–135. https://doi.org/10.1016/j.chroma.2014.10.026
   PubMed Web of Science ®Google Scholar
• Hemler, M. E. (2005). Tetraspanin functions and associated microdomains. Nature Reviews Molecular Cell Biology, 6(10), 801–811. https://doi.org/10.1038/nrm1736
   PubMed Web of Science ®Google Scholar
• Henne, W. M., Buchkovich, N. J., & Emr, S. D. (2011). The ESCRT pathway. Developmental Cell., 21(1), 77–91. https://doi.org/10.1016/j.devcel.2011.05.015
   PubMed Web of Science ®Google Scholar
• Henne, W. M., Stenmark, H., & Emr, S. D. (2013). Molecular mechanisms of the membrane sculpting ESCRT pathway. Cold Spring Harbor Perspectives in Biology, 5(9), a016766.
   PubMed Web of Science ®Google Scholar
• Hess, S. T., Girirajan, T. P., & Mason, M. D. (2006). Ultra-high resolution imaging by fluorescence photoactivation localization microscopy. Biophysical Journal., 91(11), 4258–4272. https://doi.org/10.1529/biophysj.106.091116
   PubMed Web of Science ®Google Scholar
• Hildreth, J. E. K. (2017). HIV as Trojan exosome: Immunological paradox explained? Frontiers in Immunology, 8, 1715. https://doi.org/10.3389/fimmu.2017.01715
   PubMed Web of Science ®Google Scholar
• Hinds, M. G., Smits, C., Fredericks-Short, R., Risk, J. M., Bailey, M., Huang, D. C. S., & Day, C. L. (2007). Bim, Bad and Bmf: Intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. Cell Death & Differentiation, 14(1), 128–136. https://doi.org/10.1038/sj.cdd.4401934
   PubMed Web of Science ®Google Scholar
• Hoenen, T., Shabman, R. S., Groseth, A., Herwig, A., Weber, M., Schudt, G., Dolnik, O., Basler, C. F., Becker, S., & Feldmann, H. (2012). Inclusion bodies are a site of ebolavirus replication. Journal of Virology, 86(21), 11779–11788. https://doi.org/10.1128/JVI.01525-12
   PubMed Web of Science ®Google Scholar
• Holmes, E. C. (1998). Molecular epidemiology and evolution of emerging infectious diseases. British Medical Bulletin, 54(3), 533–543. https://doi.org/10.1093/oxfordjournals.bmb.a011708
   PubMed Web of Science ®Google Scholar
• Honegger, A., Schilling, D., Bastian, S., Sponagel, J., Kuryshev, V., Sültmann, H., Scheffner, M., Hoppe-Seyler, K., & Hoppe-Seyler, F. (2015). Dependence of intracellular and exosomal microRNAs on viral E6/E7 oncogene expression in HPV-positive tumor cells. PLOS Pathogens, 11(3), e1004712. https://doi.org/10.1371/journal.ppat.1004712
   PubMed Web of Science ®Google Scholar
• Hu, L., & Dow, K. (2014). Focal seizures after instillation of cyclomydril to a neonate with congenital CMV infection. Journal of Neonatal-Perinatal Medicine, 7(2), 147–149. https://doi.org/10.3233/NPM-1476413
   PubMedGoogle Scholar
• Huang, I.-C., Bailey, C. C., Weyer, J. L., Radoshitzky, S. R., Becker, M. M., Chiang, J. J., Brass, A. L., Ahmed, A. A., Chi, X., Dong, L., Longobardi, L. E., Boltz, D., Kuhn, J. H., Elledge, S. J., Bavari, S., Denison, M. R., Choe, H., & Farzan, M. (2011). Distinct patterns of IFITM-mediated restriction of filoviruses, SARS coronavirus, and influenza A virus. PLoS Pathogens, 7(1), e1001258. https://doi.org/10.1371/journal.ppat.1001258
   PubMed Web of Science ®Google Scholar
• Hurley, J. H., & Hanson, P. I. (2010). Membrane budding and scission by the ESCRT machinery: It’s all in the neck. Nature Reviews Molecular Cell Biology, 11(8), 556–566. https://doi.org/10.1038/nrm2937
   PubMed Web of Science ®Google Scholar
• Hurwitz, S. N., Nkosi, D., Conlon, M. M., York, S. B., Liu, X., Tremblay, D. C., & Meckes, D. G. Jr. (2017). CD63 regulates Epstein-Barr virus LMP1 exosomal packaging, enhancement of vesicle production, and noncanonical NF-kappaB signaling. Journal of Virology, 91(5), e02251. https://doi.org/10.1128/JVI.02251-16
   PubMed Web of Science ®Google Scholar
• Iakoucheva, L. M., Radivojac, P., Brown, C. J., O’Connor, T. R., Sikes, J. G., Obradovic, Z., & Dunker, A. K. (2004). The importance of intrinsic disorder for protein phosphorylation. Nucleic Acids Research, 32(3), 1037–1049. https://doi.org/10.1093/nar/gkh253
   PubMed Web of Science ®Google Scholar
• Ishida, T., & Kinoshita, K. (2007). PrDOS: Prediction of disordered protein regions from amino acid sequence. Nucleic Acids Research, 35(Web Server issue), W460–464. https://doi.org/10.1093/nar/gkm363
   PubMed Web of Science ®Google Scholar
• Iwakiri, D., & Takada, K. (2010). Role of EBERs in the pathogenesis of EBV infection. Advances in Cancer Research, 107, 119–136. https://doi.org/10.1016/S0065-230X(10)07004-1
   PubMed Web of Science ®Google Scholar
• Izquierdo-Useros, N., Naranjo-Gómez, M., Archer, J., Hatch, S. C., Erkizia, I., Blanco, J., Borràs, F. E., Puertas, M. C., Connor, J. H., Fernández-Figueras, M. T., Moore, L., Clotet, B., Gummuluru, S., & Martinez-Picado, J. (2009). Capture and transfer of HIV-1 particles by mature dendritic cells converges with the exosome-dissemination pathway. Blood, 113(12), 2732–2741. https://doi.org/10.1182/blood-2008-05-158642
   PubMed Web of Science ®Google Scholar
• Izquierdo‐Useros, N., Puertas, M. C., Borràs, F. E., Blanco, J., & Martinez‐Picado, J. (2011). Exosomes and retroviruses: The chicken or the egg? Cellular Microbiology, 13(1), 10–17. https://doi.org/10.1111/j.1462-5822.2010.01542.x
   PubMed Web of Science ®Google Scholar
• Jakob, U., Kriwacki, R., & Uversky, V. N. (2014). Conditionally and transiently disordered proteins: Awakening cryptic disorder to regulate protein function. Chemical Reviews, 114(13), 6779–6805. https://doi.org/10.1021/cr400459c
   PubMed Web of Science ®Google Scholar
• Jankovičová, J., Simon, M., Antalíková, J., Cupperová, P., & Michalková, K. (2015). Role of tetraspanin CD9 molecule in fertilization of mammals. Physiological Research, 64(3), 64.
   Web of Science ®Google Scholar
• Jaworski, E., Narayanan, A., Van Duyne, R., Shabbeer-Meyering, S., Iordanskiy, S., Saifuddin, M., Das, R., Afonso, P. V., Sampey, G. C., Chung, M., Popratiloff, A., Shrestha, B., Sehgal, M., Jain, P., Vertes, A., Mahieux, R., & Kashanchi, F. (2014). Human T-lymphotropic virus type 1-infected cells secrete exosomes that contain Tax protein. Journal of Biological Chemistry, 289(32), 22284–22305. https://doi.org/10.1074/jbc.M114.549659
   PubMed Web of Science ®Google Scholar
• Jiang, D., Weidner, J. M., Qing, M., Pan, X.-B., Guo, H., Xu, C., Zhang, X., Birk, A., Chang, J., Shi, P.-Y., Block, T. M., & Guo, J.-T. (2010). Identification of five interferon-induced cellular proteins that inhibit west nile virus and dengue virus infections. Journal of Virology, 84(16), 8332–8341. https://doi.org/10.1128/JVI.02199-09
   PubMed Web of Science ®Google Scholar
• Jiang, Y., Ou, Y., & Cheng, X. (2013). Role of TSG101 in cancer. Frontiers in Bioscience, 18(1), 279–288. https://doi.org/10.2741/4099
   Google Scholar
• Johnstone, R. M. (1992). The Jeanne Manery-Fisher Memorial Lecture 1991. Maturation of reticulocytes: Formation of exosomes as a mechanism for shedding membrane proteins. Biochemistry and Cell Biology, 70(3–4), 179–190. https://doi.org/10.1139/o92-028
   PubMed Web of Science ®Google Scholar
• Johnstone, R. M., Adam, M., Hammond, J. R., Orr, L., & Turbide, C. (1987). Vesicle formation during reticulocyte maturation. Association of plasma membrane activities with released vesicles (exosomes). The Journal of Biological Chemistry, 262(19), 9412–9420.
   PubMed Web of Science ®Google Scholar
• Johnstone, R. M., Bianchini, A., & Teng, K. (1989). Reticulocyte maturation and exosome release: Transferrin receptor containing exosomes shows multiple plasma membrane functions. Blood, 74(5), 1844–1851. https://doi.org/10.1182/blood.V74.5.1844.1844
   PubMed Web of Science ®Google Scholar
• Jorda, J., Xue, B., Uversky, V. N., & Kajava, A. V. (2010). Protein tandem repeats: The more perfect, the less structured. FEBS Journal, 277(12), 2673–2682. https://doi.org/10.1111/j.1742-464X.2010.07684.x
   PubMed Web of Science ®Google Scholar
• Jørgensen, M., Baek, R., Pedersen, S., Søndergaard, E. K., Kristensen, S. R., & Varming, K. (2013). Extracellular vesicle (EV) array: Microarray capturing of exosomes and other extracellular vesicles for multiplexed phenotyping. Journal of Extracellular Vesicles, 2(1), 20920. https://doi.org/10.3402/jev.v2i0.20920
   PubMedGoogle Scholar
• Jouvenet, N. (2012). Dynamics of ESCRT proteins. Cellular and Molecular Life Sciences, 69(24), 4121–4133. https://doi.org/10.1007/s00018-012-1035-0
   PubMed Web of Science ®Google Scholar
• Jouvenet, N., Zhadina, M., Bieniasz, P. D., & Simon, S. M. (2011). Dynamics of ESCRT protein recruitment during retroviral assembly. Nature Cell Biology, 13(4), 394–401. https://doi.org/10.1038/ncb2207
   PubMed Web of Science ®Google Scholar
• Jung, K. K., Liu, X. W., Chirco, R., Fridman, R., & Kim, H. R. (2006). Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein. The EMBO Journal, 25(17), 3934–3942. https://doi.org/10.1038/sj.emboj.7601281
   PubMed Web of Science ®Google Scholar
• Kadiu, I., Narayanasamy, P., Dash, P. K., Zhang, W., & Gendelman, H. E. (2012). Biochemical and biologic characterization of exosomes and microvesicles as facilitators of HIV-1 infection in macrophages. The Journal of Immunology, 189(2), 744–754. https://doi.org/10.4049/jimmunol.1102244
   PubMed Web of Science ®Google Scholar
• Kagan, K. O., & Hamprecht, K. (2017). Cytomegalovirus infection in pregnancy. Archives of Gynecology and Obstetrics, 296(1), 15–26. https://doi.org/10.1007/s00404-017-4380-2
   PubMed Web of Science ®Google Scholar
• Kahali, B., & Ghosh, T. C. (2013). Disorderness in Escherichia coli proteome: Perception of folding fidelity and protein-protein interactions. Journal of Biomolecular Structure and Dynamics, 31(5), 472–476. https://doi.org/10.1080/07391102.2012.706071
   PubMed Web of Science ®Google Scholar
• Kalamvoki, M., Du, T., & Roizman, B. (2014). Cells infected with herpes simplex virus 1 export to uninfected cells exosomes containing STING, viral mRNAs, and microRNAs. Proceedings of the National Academy of Sciences, 111(46), E4991–4996. https://doi.org/10.1073/pnas.1419338111
   PubMed Web of Science ®Google Scholar
• Keller, S., Ridinger, J., Rupp, A. K., Janssen, J. W., & Altevogt, P. (2011). Body fluid derived exosomes as a novel template for clinical diagnostics. Journal of Translational Medicine, 9(1), 86. https://doi.org/10.1186/1479-5876-9-86
   PubMed Web of Science ®Google Scholar
• Keller, S., Sanderson, M. P., Stoeck, A., & Altevogt, P. (2006). Exosomes: From biogenesis and secretion to biological function. Immunology Letters, 107(2), 102–108. https://doi.org/10.1016/j.imlet.2006.09.005
   PubMed Web of Science ®Google Scholar
• Keren-Kaplan, T., Attali, I., Estrin, M., Kuo, L. S., Farkash, E., Jerabek-Willemsen, M., Blutraich, N., Artzi, S., Peri, A., Freed, E. O., Wolfson, H. J., & Prag, G. (2013). Structure-based in silico identification of ubiquitin-binding domains provides insights into the ALIX-V: Ubiquitin complex and retrovirus budding. The EMBO Journal, 32(4), 538–551. https://doi.org/10.1038/emboj.2013.4
   PubMed Web of Science ®Google Scholar
• Khan, S., Aspe, J. R., Asumen, M. G., Almaguel, F., Odumosu, O., Acevedo-Martinez, S., De Leon, M., Langridge, W. H. R., & Wall, N. R. (2009). Extracellular, cell-permeable survivin inhibits apoptosis while promoting proliferative and metastatic potential. British Journal of Cancer, 100(7), 1073–1086. https://doi.org/10.1038/sj.bjc.6604978
   PubMed Web of Science ®Google Scholar
• Khan, S., Bennit, H. F., & Wall, N. R. (2015). The emerging role of exosomes in survivin secretion. Histology and Histopathology, 30(1), 43–50. https://doi.org/10.14670/HH-30.43
   PubMed Web of Science ®Google Scholar
• Khan, S., Jutzy, J. M., Aspe, J. R., McGregor, D. W., Neidigh, J. W., & Wall, N. R. (2011). Survivin is released from cancer cells via exosomes. Apoptosis, 16(1), 1–12. https://doi.org/10.1007/s10495-010-0534-4
   PubMed Web of Science ®Google Scholar
• Khatun, M., & Ray, R. B. (2019). Mechanisms underlying hepatitis C virus-associated hepatic fibrosis. Cells, 8(10), 1249. https://doi.org/10.3390/cells8101249
   Web of Science ®Google Scholar
• Kirchdoerfer, R. N., Abelson, D. M., Li, S., Wood, M. R., & Saphire, E. O. (2015). Assembly of the Ebola virus nucleoprotein from a chaperoned VP35 complex. Cell Reports, 12(1), 140–149. https://doi.org/10.1016/j.celrep.2015.06.003
   PubMed Web of Science ®Google Scholar
• Klar, T. A., & Hell, S. W. (1999). Subdiffraction resolution in far-field fluorescence microscopy. Optics Letters, 24(14), 954–956. https://doi.org/10.1364/OL.24.000954
   PubMed Web of Science ®Google Scholar
• Kobayashi, T., Vischer, U. M., Rosnoblet, C., Lebrand, C., Lindsay, M., Parton, R. G., Kruithof, E. K. O., & Gruenberg, J. (2000). The tetraspanin CD63/lamp3 cycles between endocytic and secretory compartments in human endothelial cells. Molecular Biology of the Cell, 11(5), 1829–1843. https://doi.org/10.1091/mbc.11.5.1829
   PubMed Web of Science ®Google Scholar
• Konadu, K A., Chu, J., Huang, M. B., Amancha, P. K., Armstrong, W., Powell, M. D., Villinger, F., & Bond, V. C. (2015). Association of cytokines with exosomes in the plasma of HIV-1-seropositive individuals. Journal of Infectious Diseases, 211(11), 1712–1716. https://doi.org/10.1093/infdis/jiu676
   PubMed Web of Science ®Google Scholar
• Korneta, I., & Bujnicki, J. M. (2012). Intrinsic disorder in the human spliceosomal proteome. PLoS Computational Biology, 8(8), e1002641. https://doi.org/10.1371/journal.pcbi.1002641
   PubMed Web of Science ®Google Scholar
• Kowal, J., Arras, G., Colombo, M., Jouve, M., Morath, J. P., Primdal-Bengtson, B., Dingli, F., Loew, D., Tkach, M., & Théry, C. (2016). Proteomic comparison defines novel markers to characterize heterogeneous populations of extracellular vesicle subtypes. Proceedings of the National Academy of Sciences, 113(8), E968–E977 https://doi.org/10.1073/pnas.1521230113
   PubMed Web of Science ®Google Scholar
• Kraemer, M. U. G., Sinka, M. E., Duda, K. A., Mylne, A. Q. N., Shearer, F. M., Barker, C. M., Moore, C. G., Carvalho, R. G., Coelho, G. E., Van Bortel, W., Hendrickx, G., Schaffner, F., Elyazar, I. R. F., Teng, H.-J., Brady, O. J., Messina, J. P., Pigott, D. M., Scott, T. W., Smith, D. L., … Hay, S. I. (2015). The global distribution of the arbovirus vectors Aedes aegypti and Ae. albopictus. eLife, 4, e08347. https://doi.org/10.7554/eLife.08347
   PubMed Web of Science ®Google Scholar
• Krasowski, M. D., Reschly, E. J., & Ekins, S. (2008). Intrinsic disorder in nuclear hormone receptors. Journal of Proteome Research, 7(10), 4359–4372. https://doi.org/10.1021/pr8003024
   PubMed Web of Science ®Google Scholar
• Lai, R. C., Yeo, R. W., Tan, K. H., & Lim, S. K. (2013). Exosomes for drug delivery: A novel application for the mesenchymal stem cell. Biotechnology Advances, 31(5), 543–551. https://doi.org/10.1016/j.biotechadv.2012.08.008
   PubMed Web of Science ®Google Scholar
• Laina, I., Syriopoulou, V. P., Daikos, G. L., Roma, E. S., Papageorgiou, F., Kakourou, T., & Theodoridou, M. (2010). Febrile seizures and primary human herpesvirus 6 infection. Pediatric Neurology, 42(1), 28–31. https://doi.org/10.1016/j.pediatrneurol.2009.07.016
   PubMed Web of Science ®Google Scholar
• Lamparski, H. G., Metha-Damani, A., Yao, J.-Y., Patel, S., Hsu, D.-H., Ruegg, C., & Le Pecq, J.-B. (2002). Production and characterization of clinical grade exosomes derived from dendritic cells. Journal of Immunological Methods, 270(2), 211–226. https://doi.org/10.1016/S0022-1759(02)00330-7
   PubMed Web of Science ®Google Scholar
• Lane, R. E., Korbie, D., Trau, M., & Hill, M. M. (2017). Purification protocols for extracellular vesicles. Methods in Molecular Biology (Clifton, NJ.), 1660, 111–130. https://doi.org/10.1007/978-1-4939-7253-1_10
   PubMedGoogle Scholar
• Lanford, R. E., Feng, Z., Chavez, D., Guerra, B., Brasky, K. M., Zhou, Y., Yamane, D., Perelson, A. S., Walker, C. M., & Lemon, S. M. (2011). Acute hepatitis A virus infection is associated with a limited type I interferon response and persistence of intrahepatic viral RNA. Proceedings of the National Academy of Sciences, 108(27), 11223–11228. https://doi.org/10.1073/pnas.1101939108
   PubMed Web of Science ®Google Scholar
• Lee, J.-H., Schierer, S., Blume, K., Dindorf, J., Wittki, S., Xiang, W., Ostalecki, C., Koliha, N., Wild, S., Schuler, G., Fackler, O. T., Saksela, K., Harrer, T., & Baur, A. S. (2016). HIV-Nef and ADAM17-containing plasma extracellular vesicles induce and correlate with immune pathogenesis in chronic HIV infection. EBioMedicine, 6, 103–113. https://doi.org/10.1016/j.ebiom.2016.03.004
   PubMed Web of Science ®Google Scholar
• Lemon, S. M. (1985). Type A viral hepatitis. New developments in an old disease. New England Journal of Medicine, 313(17), 1059–1067. https://doi.org/10.1056/NEJM198510243131706
   PubMed Web of Science ®Google Scholar
• Lener, T., Gimona, M., Aigner, L., Börger, V., Buzas, E., Camussi, G., Chaput, N., Chatterjee, D., Court, F. A., Portillo, H. A., O’Driscoll, L., Fais, S., Falcon-Perez, J. M., Felderhoff-Mueser, U., Fraile, L., Gho, Y. S., Görgens, A., Gupta, R. C., Hendrix, A., … Giebel, B. (2015). Applying extracellular vesicles based therapeutics in clinical trials: An ISEV position paper. Journal of Extracellular Vesicles, 4(1), 30087. https://doi.org/10.3402/jev.v4.30087
   PubMed Web of Science ®Google Scholar
• Levy, S. (2014). Function of the tetraspanin molecule CD81 in B and T cells. Immunologic Research, 58(2–3), 179–185. https://doi.org/10.1007/s12026-014-8490-7
   PubMed Web of Science ®Google Scholar
• Levy, S., & Shoham, T. (2005). The tetraspanin web modulates immune-signalling complexes. Nature Reviews Immunology, 5(2), 136–148. https://doi.org/10.1038/nri1548
   PubMed Web of Science ®Google Scholar
• Li, K., Wong, D. K., Hong, K. Y., & Raffai, R. L. (2018). Cushioned-density gradient ultracentrifugation (C-DGUC): A refined and high performance method for the isolation, characterization, and use of exosomes. Methods in Molecular Biology (Clifton, NJ), 1740, 69–83. https://doi.org/10.1007/978-1-4939-7652-2_7
   PubMedGoogle Scholar
• Lieutaud, P., Ferron, F., Uversky, A. V., Kurgan, L., Uversky, V. N., & Longhi, S. (2016). How disordered is my protein and what is its disorder for? A guide through the “dark side” of the protein universe. Intrinsically Disordered Proteins, 4(1), e1259708. https://doi.org/10.1080/21690707.2016.1259708
   PubMedGoogle Scholar
• Lin, Z., & Flemington, E. K. (2011). miRNAs in the pathogenesis of oncogenic human viruses. Cancer Letters, 305(2), 186–199. https://doi.org/10.1016/j.canlet.2010.08.018
   PubMed Web of Science ®Google Scholar
• Liu, Z., Zhang, X., Yu, Q., & He, J. J. (2014). Exosome-associated hepatitis C virus in cell cultures and patient plasma. Biochemical and Biophysical Research Communications, 455(3–4), 218–222. https://doi.org/10.1016/j.bbrc.2014.10.146
   PubMed Web of Science ®Google Scholar
• Logozzi, M., De Milito, A., Lugini, L., Borghi, M., Calabrò, L., Spada, M., Perdicchio, M., Marino, M. L., Federici, C., Iessi, E., Brambilla, D., Venturi, G., Lozupone, F., Santinami, M., Huber, V., Maio, M., Rivoltini, L., & Fais, S. (2009). High levels of exosomes expressing CD63 and caveolin-1 in plasma of melanoma patients. PloS One, 4(4), e5219. https://doi.org/10.1371/journal.pone.0005219
   PubMed Web of Science ®Google Scholar
• Longatti, A. (2015). The dual role of exosomes in hepatitis A and C virus transmission and viral immune activation. Viruses, 7(12), 6707–6715. https://doi.org/10.3390/v7122967
   PubMed Web of Science ®Google Scholar
• Lötvall, J., Hill, A. F., Hochberg, F., Buzás, E. I., Di Vizio, D., Gardiner, C., Gho, Y. S., Kurochkin, I. V., Mathivanan, S., Quesenberry, P., Sahoo, S., Tahara, H., Wauben, M. H., Witwer, K. W., & Théry, C. (2014). Minimal experimental requirements for definition of extracellular vesicles and their functions: A position statement from the International Society for Extracellular Vesicles. Journal of Extracellular Vesicles, 3(1), 26913. https://doi.org/10.3402/jev.v3.26913
   PubMedGoogle Scholar
• Lozano-Ramos, I., Bancu, I., Oliveira-Tercero, A., Armengol, M. P., Menezes-Neto, A., Portillo, H. A. D., Lauzurica-Valdemoros, R., & Borràs, F. E. (2015). Size-exclusion chromatography-based enrichment of extracellular vesicles from urine samples. Journal of Extracellular Vesicles, 4(1), 27369. https://doi.org/10.3402/jev.v4.27369
   PubMed Web of Science ®Google Scholar
• Lu, J., Pan, Q., Rong, L., Liu, S.-L., & Liang, C. (2011). The IFITM proteins inhibit HIV-1 infection. Journal of Virology, 85(5), 2126–2137. https://doi.org/10.1128/JVI.01531-10
   PubMed Web of Science ®Google Scholar
• Ludwig, A.-K., & Giebel, B. (2012). Exosomes: Small vesicles participating in intercellular communication. International Journal of Biochemistry & Cell Biology., 44(1), 11–15. https://doi.org/10.1016/j.biocel.2011.10.005
   PubMed Web of Science ®Google Scholar
• Mack, M., Kleinschmidt, A., Brühl, H., Klier, C., Nelson, P. J., Cihak, J., Plachý, J., Stangassinger, M., Erfle, V., & Schlöndorff, D. (2000). Transfer of the chemokine receptor CCR5 between cells by membrane-derived microparticles: A mechanism for cellular human immunodeficiency virus 1 infection. Nature Medicine, 6(7), 769–775. https://doi.org/10.1038/77498
   PubMed Web of Science ®Google Scholar
• Malik, S., & Eugenin, E. A. (2016). Mechanisms of HIV neuropathogenesis: Role of cellular communication systems. Current HIV Research, 14(5), 400–411. https://doi.org/10.2174/1570162X14666160324124558
   PubMed Web of Science ®Google Scholar
• Martin-Serrano, J., Eastman, S. W., Chung, W., & Bieniasz, P. D. (2005). HECT ubiquitin ligases link viral and cellular PPXY motifs to the vacuolar protein-sorting pathway. Journal of Cell Biology, 168(1), 89–101. https://doi.org/10.1083/jcb.200408155
   PubMed Web of Science ®Google Scholar
• Martin-Serrano, J., Zang, T., & Bieniasz, P. D. (2001). HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nature Medicine, 7(12), 1313–1319. https://doi.org/10.1038/nm1201-1313
   PubMed Web of Science ®Google Scholar
• Martin-Serrano, J., Zang, T., & Bieniasz, P. D. (2003). Role of ESCRT-I in retroviral budding. Journal of Virology, 77(8), 4794–4804. https://doi.org/10.1128/JVI.77.8.4794-4804.2003
   PubMed Web of Science ®Google Scholar
• Martin, A., & Lemon, S. M. (2006). Hepatitis A virus: From discovery to vaccines. Hepatology, 43(Suppl 1), S164–S172. https://doi.org/10.1002/hep.21052
   PubMedGoogle Scholar
• Martins, S. D. T., Kuczera, D., Lötvall, J., Bordignon, J., & Alves, L. R. (2018). Characterization of dendritic cell-derived extracellular vesicles during dengue virus infection. Frontiers in Microbiology, 9, 1792. https://doi.org/10.3389/fmicb.2018.01792
   PubMed Web of Science ®Google Scholar
• Mashouri, L., Yousefi, H., Aref, A. R., Ahadi, A. M., Molaei, F., & Alahari, S. K. (2019). Exosomes: Composition, biogenesis, and mechanisms in cancer metastasis and drug resistance. Molecular Cancer, 18(1), 75. https://doi.org/10.1186/s12943-019-0991-5
   PubMed Web of Science ®Google Scholar
• Mathieu, M., Martin-Jaular, L., Lavieu, G., & Thery, C. (2019). Specificities of secretion and uptake of exosomes and other extracellular vesicles for cell-to-cell communication. Nature Cell Biology, 21(1), 9–17. https://doi.org/10.1038/s41556-018-0250-9
   PubMed Web of Science ®Google Scholar
• Matsuo, H., Chevallier, J., Mayran, N., Le Blanc, I., Ferguson, C., Fauré, J., Blanc, N. S., Matile, S., Dubochet, J., Sadoul, R., Parton, R. G., Vilbois, F., & Sadoul, R. (2004). Role of LBPA and Alix in multivesicular liposome formation and endosome organization. Science, 303(5657), 531–534. https://doi.org/10.1126/science.1092425
   PubMed Web of Science ®Google Scholar
• McCullough, J., Colf, L. A., & Sundquist, W. I. (2013). Membrane fission reactions of the mammalian ESCRT pathway. Annual Review of Biochemistry, 82(1), 663–692. https://doi.org/10.1146/annurev-biochem-072909-101058
   PubMedGoogle Scholar
• Meckes, D. G., Gunawardena, H. P., Dekroon, R. M., Heaton, P. R., Edwards, R. H., Ozgur, S., Griffith, J. D., Damania, B., & Raab-Traub, N. (2013). Modulation of B-cell exosome proteins by gamma herpesvirus infection. Proceedings of the National Academy of Sciences, 110(31), E2925–2933. https://doi.org/10.1073/pnas.1303906110
   PubMed Web of Science ®Google Scholar
• Meckes, D. G., Jr., Shair, K. H., Marquitz, A. R., Kung, C. P., Edwards, R. H., & Raab-Traub, N. (2010). Human tumor virus utilizes exosomes for intercellular communication. Proceedings of the National Academy of Sciences, 107(47), 20370–20375. https://doi.org/10.1073/pnas.1014194107
   PubMed Web of Science ®Google Scholar
• Meckes, D. G., & Raab-Traub, N. (2011). Microvesicles and viral infection. Journal of Virology, 85(24), 12844–12854. https://doi.org/10.1128/JVI.05853-11
   PubMed Web of Science ®Google Scholar
• Medintz, I. L., Uyeda, H. T., Goldman, E. R., & Mattoussi, H. (2005). Quantum dot bioconjugates for imaging, labelling and sensing. Nature Materials, 4(6), 435–446. https://doi.org/10.1038/nmat1390
   PubMed Web of Science ®Google Scholar
• Meehan, B., Rak, J., & Di Vizio, D. (2016). Oncosomes - large and small: What are they, where they came from? Journal of Extracellular Vesicles, 5(1), 33109. https://doi.org/10.3402/jev.v5.33109
   PubMed Web of Science ®Google Scholar
• Meister, M., Banfer, S., Gartner, U., Koskimies, J., Amaddii, M., Jacob, R., & Tikkanen, R. (2017). Regulation of cargo transfer between ESCRT-0 and ESCRT-I complexes by flotillin-1 during endosomal sorting of ubiquitinated cargo. Oncogenesis, 6(6), e344–e344. https://doi.org/10.1038/oncsis.2017.47
   PubMedGoogle Scholar
• Melentijevic, I., Toth, M. L., Arnold, M. L., Guasp, R. J., Harinath, G., Nguyen, K. C., Taub, D., Parker, J. A., Neri, C., Gabel, C. V., Hall, D. H., & Driscoll, M. (2017). C. elegans neurons jettison protein aggregates and mitochondria under neurotoxic stress. Nature, 542(7641), 367–371. https://doi.org/10.1038/nature21362
   PubMed Web of Science ®Google Scholar
• Melton, L. (2004). Proteomics in multiplex. Nature, 429(6987), 105–107. https://doi.org/10.1038/429101a
   Web of Science ®Google Scholar
• Mesri, E. A., Cesarman, E., & Boshoff, C. (2010). Kaposi’s sarcoma and its associated herpesvirus. Nature Reviews Cancer, 10(10), 707–719. https://doi.org/10.1038/nrc2888
   PubMed Web of Science ®Google Scholar
• Mi, S., Qin, X.-W., Lin, Y.-F., He, J., Chen, N.-N., Liu, C., Weng, S.-P., He, J.-G., & Guo, C.-J. (2016). Budding of tiger frog virus (an iridovirus) from HepG2 cells via three ways recruits the ESCRT pathway. Scientific Reports, 6(1), 26581. https://doi.org/10.1038/srep26581
   PubMedGoogle Scholar
• Midic, U., & Obradovic, Z. (2012). Intrinsic disorder in putative protein sequences. Proteome Science, 10 (Suppl 1), S19. https://doi.org/10.1186/1477-5956-10-S1-S19
   PubMedGoogle Scholar
• Mishra, R., Lata, S., Ali, A., & Banerjea, A. C. (2019). Dengue haemorrhagic fever: A job done via exosomes? Emerging Microbes & Infections, 8(1), 1626–1635. https://doi.org/10.1080/22221751.2019.1685913
   PubMed Web of Science ®Google Scholar
• Mitchell, P., Petfalski, E., Shevchenko, A., Mann, M., & Tollervey, D. (1997). The exosome: A conserved eukaryotic RNA processing complex containing multiple 3’–>5’ exoribonucleases. Cell, 91(4), 457–466. https://doi.org/10.1016/S0092-8674(00)80432-8
   PubMed Web of Science ®Google Scholar
• Momen-Heravi, F., Balaj, L., Alian, S., Mantel, P.-Y., Halleck, A. E., Trachtenberg, A. J., Soria, C. E., Oquin, S., Bonebreak, C. M., Saracoglu, E., Skog, J., & Kuo, W. P. (2013). Current methods for the isolation of extracellular vesicles. Biological Chemistry, 394(10), 1253–1262. https://doi.org/10.1515/hsz-2013-0141
   PubMed Web of Science ®Google Scholar
• Momen-Heravi, F., Balaj, L., Alian, S., Trachtenberg, A. J., Hochberg, F. H., Skog, J., & Kuo, W. P. (2012). Impact of biofluid viscosity on size and sedimentation efficiency of the isolated microvesicles. Frontiers in Physiology, 3, 162. https://doi.org/10.3389/fphys.2012.00162
   PubMed Web of Science ®Google Scholar
• Morello, M., Minciacchi, V., de Candia, P., Yang, J., Posadas, E., Kim, H., Griffiths, D., Bhowmick, N., Chung, L., Gandellini, P., Freeman, M., Demichelis, F., & DiVizio, D. (2013). Large oncosomes mediate intercellular transfer of functional microRNA. Cell Cycle, 12(22), 3526–3536. https://doi.org/10.4161/cc.26539
   PubMed Web of Science ®Google Scholar
• Morgello, S., & Simpson, D. M. (1994). Multifocal cytomegalovirus demyelinative polyneuropathy associated with AIDS. Muscle & Nerve, 17(2), 176–182. https://doi.org/10.1002/mus.880170208
   PubMed Web of Science ®Google Scholar
• Mori, Y., Koike, M., Moriishi, E., Kawabata, A., Tang, H., Oyaizu, H., Uchiyama, Y., & Yamanishi, K. (2008). Human herpesvirus-6 induces MVB formation, and virus egress occurs by an exosomal release pathway. Traffic, 9(10), 1728–1742. https://doi.org/10.1111/j.1600-0854.2008.00796.x
   PubMed Web of Science ®Google Scholar
• MüNger, K., Baldwin, A., Edwards, K. M., Hayakawa, H., Nguyen, C. L., Owens, M., Grace, M., & Huh, K. (2004). Mechanisms of human papillomavirus-induced oncogenesis. Journal of Virology, 78(21), 11451–11460. https://doi.org/10.1128/JVI.78.21.11451-11460.2004
   PubMed Web of Science ®Google Scholar
• Murrow, L., & Debnath, J. (2015). ATG12-ATG3 connects basal autophagy and late endosome function. Autophagy, 11(6), 961–962. https://doi.org/10.1080/15548627.2015.1040976
   PubMed Web of Science ®Google Scholar
• Mustafa, M. S., Rasotgi, V., Jain, S., & Gupta, V. (2015). Discovery of fifth serotype of dengue virus (DENV-5): A new public health dilemma in dengue control. Medical Journal Armed Forces India, 71(1), 67–70. https://doi.org/10.1016/j.mjafi.2014.09.011
   PubMedGoogle Scholar
• Nabhan, J. F., Hu, R., Oh, R. S., Cohen, S. N., & Lu, Q. (2012). Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein. Proceedings of the National Academy of Sciences, 109(11), 4146–4151. https://doi.org/10.1073/pnas.1200448109
   PubMed Web of Science ®Google Scholar
• Nanbo, A., Kawanishi, E., Yoshida, R., & Yoshiyama, H. (2013). Exosomes derived from Epstein-Barr virus-infected cells are internalized via caveola-dependent endocytosis and promote phenotypic modulation in target cells. Journal of Virology, 87(18), 10334–10347. https://doi.org/10.1128/JVI.01310-13
   PubMed Web of Science ®Google Scholar
• Narayanan, A., Iordanskiy, S., Das, R., Van Duyne, R., Santos, S., Jaworski, E., Guendel, I., Sampey, G., Dalby, E., Iglesias-Ussel, M., Popratiloff, A., Hakami, R., Kehn-Hall, K., Young, M., Subra, C., Gilbert, C., Bailey, C., Romerio, F., & Kashanchi, F. (2013). Exosomes derived from HIV-1-infected cells contain trans-activation response element RNA. Journal of Biological Chemistry, 288(27), 20014–20033. https://doi.org/10.1074/jbc.M112.438895
   PubMed Web of Science ®Google Scholar
• Negro, F., & Alberti, A. (2011). The global health burden of hepatitis C virus infection. Liver International, 31 (Suppl 2), 1–3. https://doi.org/10.1111/j.1478-3231.2011.02537.x
   PubMed Web of Science ®Google Scholar
• Niu, Z., Pang, R. T. K., Liu, W., Li, Q., Cheng, R., & Yeung, W. S. B. (2017). Polymer-based precipitation preserves biological activities of extracellular vesicles from an endometrial cell line. PloS One, 12(10), e0186534. https://doi.org/10.1371/journal.pone.0186534
   PubMed Web of Science ®Google Scholar
• Noda, T., Hagiwara, K., Sagara, H., & Kawaoka, Y. (2010). Characterization of the Ebola virus nucleoprotein-RNA complex. Journal of General Virology., 91(6), 1478–1483. https://doi.org/10.1099/vir.0.019794-0
   PubMedGoogle Scholar
• Nolte, E., Cremer, T., Gallo, R. C., & Margolis, L. B. (2016). Extracellular vesicles and viruses: Are they close relatives? Proceedings of the National Academy of Sciences, 113(33), 9155–9161. https://doi.org/10.1073/pnas.1605146113
   PubMed Web of Science ®Google Scholar
• Nordin, J. Z., Lee, Y., Vader, P., Mäger, I., Johansson, H. J., Heusermann, W., Wiklander, O. P. B., Hällbrink, M., Seow, Y., Bultema, J. J., Gilthorpe, J., Davies, T., Fairchild, P. J., Gabrielsson, S., Meisner-Kober, N. C., Lehtiö, J., Smith, C. I. E., Wood, M. J. A., & Andaloussi, S. E. (2015). Ultrafiltration with size-exclusion liquid chromatography for high yield isolation of extracellular vesicles preserving intact biophysical and functional properties. Nanomedicine, 11(4), 879–883. https://doi.org/10.1016/j.nano.2015.01.003
   PubMed Web of Science ®Google Scholar
• Oates, M. E., Romero, P., Ishida, T., Ghalwash, M., Mizianty, M. J., Xue, B., Dosztányi, Z., Uversky, V. N., Obradovic, Z., Kurgan, L., Dunker, A. K., & Gough, J. (2012). D(2)P(2): Database of disordered protein predictions. Nucleic Acids Research, 41(D1), D508–516. https://doi.org/10.1093/nar/gks1226
   PubMed Web of Science ®Google Scholar
• Obradovic, Z., Peng, K., Vucetic, S., Radivojac, P., & Dunker, A. K. (2005). Exploiting heterogeneous sequence properties improves prediction of protein disorder. Proteins: Structure, Function, and Bioinformatics, 61(S7), 176–182. https://doi.org/10.1002/prot.20735
   PubMedGoogle Scholar
• Oeyen, E., Van Mol, K., Baggerman, G., Willems, H., Boonen, K., Rolfo, C., Pauwels, P., Jacobs, A., Schildermans, K., Cho, W. C., & Mertens, I. (2018). Ultrafiltration and size exclusion chromatography combined with asymmetrical-flow field-flow fractionation for the isolation and characterisation of extracellular vesicles from urine. Journal of Extracellular Vesicles, 7(1), 1490143. https://doi.org/10.1080/20013078.2018.1490143
   PubMed Web of Science ®Google Scholar
• Oldfield, C. J., Cheng, Y., Cortese, M. S., Romero, P., Uversky, V. N., & Dunker, A. K. (2005). Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry, 44(37), 12454–12470. https://doi.org/10.1021/bi050736e
   PubMed Web of Science ®Google Scholar
• Ostman, C., & Chacko, B. (2019). Guillain-Barre syndrome post renal transplant: A systematic review. Transplant Infectious Disease, 21(1), e13021. https://doi.org/10.1111/tid.13021
   PubMed Web of Science ®Google Scholar
• Osuna-Ramos, J. F., Reyes-Ruiz, J. M., & del Ángel, R. M. (2018). The role of host cholesterol during flavivirus infection. Front Cell Infect Microbiol, 8, 388. https://doi.org/10.3389/fcimb.2018.00388
   PubMed Web of Science ®Google Scholar
• Ota, M., Serada, S., Naka, T., & Mori, Y. (2014). MHC class I molecules are incorporated into human herpesvirus-6 viral particles and released into the extracellular environment. Microbiology and Immunology, 58(2), 119–125. https://doi.org/10.1111/1348-0421.12121
   PubMed Web of Science ®Google Scholar
• Pan, B. T., & Johnstone, R. M. (1983). Fate of the transferrin receptor during maturation of sheep reticulocytes in vitro: Selective externalization of the receptor. Cell, 33(3), 967–978. https://doi.org/10.1016/0092-8674(83)90040-5
   PubMed Web of Science ®Google Scholar
• Pan, B. T., Teng, K., Wu, C., Adam, M., & Johnstone, R. M. (1985). Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes. The Journal of Cell Biology, 101(3), 942–948. https://doi.org/10.1083/jcb.101.3.942
   PubMed Web of Science ®Google Scholar
• Pancsa, R., & Tompa, P. (2012). Structural disorder in eukaryotes. PloS One, 7(4), e34687. https://doi.org/10.1371/journal.pone.0034687
   PubMed Web of Science ®Google Scholar
• Park, A., Yun, T., Vigant, F., Pernet, O., Won, S. T., Dawes, B. E., Bartkowski, W., Freiberg, A. N., & Lee, B. (2016). Nipah virus C protein recruits Tsg101 to promote the efficient release of virus in an ESCRT-dependent pathway. PLOS Pathogens, 12(5), e1005659. https://doi.org/10.1371/journal.ppat.1005659
   PubMed Web of Science ®Google Scholar
• Parra, G. I., Azure, J., Fischer, R., Bok, K., Sandoval-Jaime, C., Sosnovtsev, S. V., Sander, P., & Green, K. Y. (2013). Identification of a broadly cross-reactive epitope in the inner shell of the norovirus capsid. PloS One, 8(6), e67592. https://doi.org/10.1371/journal.pone.0067592
   PubMed Web of Science ®Google Scholar
• Pashkova, N., Gakhar, L., Winistorfer, S. C., Sunshine, A. B., Rich, M., Dunham, M. J., Yu, L., & Piper, R. C. (2013). The yeast Alix homolog Bro1 functions as a ubiquitin receptor for protein sorting into multivesicular endosomes. Developmental Cell., 25(5), 520–533. https://doi.org/10.1016/j.devcel.2013.04.007
   PubMed Web of Science ®Google Scholar
• Pawliczek, T., & Crump, C. M. (2009). Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression. Journal of Virology, 83(21), 11254–11264. https://doi.org/10.1128/JVI.00574-09
   PubMed Web of Science ®Google Scholar
• Pegtel, D. M., Cosmopoulos, K., Thorley-Lawson, D. A., van Eijndhoven, M. A. J., Hopmans, E. S., Lindenberg, J. L., de Gruijl, T. D., Wurdinger, T., & Middeldorp, J. M. (2010). Functional delivery of viral miRNAs via exosomes. Proceedings of the National Academy of Sciences, 107(14), 6328–6333. https://doi.org/10.1073/pnas.0914843107
   PubMed Web of Science ®Google Scholar
• Pegtel, D. M., van de Garde, M. D., & Middeldorp, J. M. (2011). Viral miRNAs exploiting the endosomal-exosomal pathway for intercellular cross-talk and immune evasion. Biochimica et Biophysica Acta, 1809(11–12), 715–721. https://doi.org/10.1016/j.bbagrm.2011.08.002
   PubMed Web of Science ®Google Scholar
• Pejaver, V., Hsu, W. L., Xin, F., Dunker, A. K., Uversky, V. N., & Radivojac, P. (2014). The structural and functional signatures of proteins that undergo multiple events of post-translational modification. Protein Science, 23(8), 1077–1093. https://doi.org/10.1002/pro.2494
   PubMed Web of Science ®Google Scholar
• Pelchen-Matthews, A., Raposo, G., & Marsh, M. (2004). Endosomes, exosomes and Trojan viruses. Trends in Microbiology, 12(7), 310–316. https://doi.org/10.1016/j.tim.2004.05.004
   PubMed Web of Science ®Google Scholar
• Peng, K., Radivojac, P., Vucetic, S., Dunker, A. K., & Obradovic, Z. (2006). Length-dependent prediction of protein intrinsic disorder. BMC Bioinformatics, 7(1), 208. https://doi.org/10.1186/1471-2105-7-208
   PubMedGoogle Scholar
• Peng, Z., Xue, B., Kurgan, L., & Uversky, V. N. (2013). Resilience of death: Intrinsic disorder in proteins involved in the programmed cell death. Cell Death & Differentiation, 20(9), 1257–1267. https://doi.org/10.1038/cdd.2013.65
   PubMed Web of Science ®Google Scholar
• Peng, Z., Yan, J., Fan, X., Mizianty, M. J., Xue, B., Wang, K., Hu, G., Uversky, V. N., & Kurgan, L. (2015). Exceptionally abundant exceptions: Comprehensive characterization of intrinsic disorder in all domains of life. Cellular and Molecular Life Sciences, 72(1), 137–151. https://doi.org/10.1007/s00018-014-1661-9
   PubMed Web of Science ®Google Scholar
• Pentony, M. M., & Jones, D. T. (2010). Modularity of intrinsic disorder in the human proteome. Proteins: Structure, Function, and Bioinformatics, 78(1), 212–221. https://doi.org/10.1002/prot.22504
   PubMed Web of Science ®Google Scholar
• Petrarca, L., Nenna, R., Frassanito, A., Pierangeli, A., Leonardi, S., Scagnolari, C., Antonelli, G., Papoff, P., Moretti, C., & Midulla, F. (2018). Acute bronchiolitis: Influence of viral co-infection in infants hospitalized over 12 consecutive epidemic seasons. Journal of Medical Virology, 90(4), 631–638. https://doi.org/10.1002/jmv.24994
   PubMed Web of Science ®Google Scholar
• Phillips, J. B., Smit, X., Zoysa, N. D., Afoke, A., & Brown, R. A. (2004). Peripheral nerves in the rat exhibit localized heterogeneity of tensile properties during limb movement. The Journal of Physiology, 557(3), 879–887. https://doi.org/10.1113/jphysiol.2004.061804
   PubMed Web of Science ®Google Scholar
• Pleet, M. L., DeMarino, C., Lepene, B., Aman, M. J., & Kashanchi, F. (2017). The role of exosomal VP40 in Ebola virus disease. NA and Cell Bioldogy, 36(4), 243–248. https://doi.org/10.1089/dna.2017.3639
   Google Scholar
• Pleet, M. L., DeMarino, C., Stonier, S. W., Dye, J. M., Jacobson, S., Aman, M. J., & Kashanchi, F. (2019). Extracellular vesicles and ebola virus: A new mechanism of immune evasion. Viruses, 11(5), 410. https://doi.org/10.3390/v11050410
   Web of Science ®Google Scholar
• Pleet, M. L., Erickson, J., DeMarino, C., Barclay, R. A., Cowen, M., Lepene, B., Liang, J., Kuhn, J. H., Prugar, L., Stonier, S. W., Dye, J. M., Zhou, W., Liotta, L. A., Aman, M. J., & Kashanchi, F. (2018). Ebola virus VP40 modulates cell cycle and biogenesis of extracellular vesicles. The Journal of Infectious Diseases, 218(suppl_5), S365–S387. https://doi.org/10.1093/infdis/jiy472
   PubMedGoogle Scholar
• Pleet, M. L., Mathiesen, A., DeMarino, C., Akpamagbo, Y. A., Barclay, R. A., Schwab, A., Iordanskiy, S., Sampey, G. C., Lepene, B., Nekhai, S., Aman, M. J., & Kashanchi, F. (2016). Ebola VP40 in exosomes can cause immune cell dysfunction. Frontiers in Microbiology, 7, 1765. https://doi.org/10.3389/fmicb.2016.01765
   PubMed Web of Science ®Google Scholar
• Pols, M. S., & Klumperman, J. (2009). Trafficking and function of the tetraspanin CD63. Experimental Cell Research, 315(9), 1584–1592. https://doi.org/10.1016/j.yexcr.2008.09.020
   PubMed Web of Science ®Google Scholar
• Powell, M. K., Benková, K., Selinger, P., Dogoši, M., Kinkorová Luňáčková, I., Koutníková, H., Laštíková, J., Roubíčková, A., Špůrková, Z., Laclová, L., Eis, V., Šach, J., & Heneberg, P. (2016). Opportunistic infections in HIV-infected patients differ strongly in frequencies and spectra between patients with low CD4+ cell counts examined postmortem and compensated patients examined antemortem irrespective of the HAART era. PloS One, 11(9), e0162704. https://doi.org/10.1371/journal.pone.0162704
   PubMed Web of Science ®Google Scholar
• Qin, J., & Xu, Q. (2014). Functions and application of exosomes. Acta Poloniae Pharmaceutica, 71(4), 537–543.
   PubMed Web of Science ®Google Scholar
• Raab-Traub, N. (2012). Novel mechanisms of EBV-induced oncogenesis. Current Opinion in Virology, 2(4), 453–458. https://doi.org/10.1016/j.coviro.2012.07.001
   PubMed Web of Science ®Google Scholar
• Raab-Traub, N., & Dittmer, D. P. (2017). Viral effects on the content and function of extracellular vesicles. Nature Reviews Microbiology, 15(9), 559–572. https://doi.org/10.1038/nrmicro.2017.60
   PubMed Web of Science ®Google Scholar
• Radivojac, P., Iakoucheva, L. M., Oldfield, C. J., Obradovic, Z., Uversky, V. N., & Dunker, A. K. (2007). Intrinsic disorder and functional proteomics. Biophysical Journal, 92(5), 1439–1456. https://doi.org/10.1529/biophysj.106.094045
   PubMed Web of Science ®Google Scholar
• Ramakrishnaiah, V., Thumann, C., Fofana, I., Habersetzer, F., Pan, Q., de Ruiter, P. E., Willemsen, R., Demmers, J. A. A., Stalin Raj, V., Jenster, G., Kwekkeboom, J., Tilanus, H. W., Haagmans, B. L., Baumert, T. F., & van der Laan, L. J. W. (2013). Exosome-mediated transmission of hepatitis C virus between human hepatoma Huh7.5 cells. Proceedings of the National Academy of Sciences, 110(32), 13109–13113. https://doi.org/10.1073/pnas.1221899110
   PubMed Web of Science ®Google Scholar
• Raposo, G., Nijman, H. W., Stoorvogel, W., Liejendekker, R., Harding, C. V., Melief, C. J., & Geuze, H. J. (1996). B lymphocytes secrete antigen-presenting vesicles. The Journal of Experimental Medicine, 183(3), 1161–1172. https://doi.org/10.1084/jem.183.3.1161
   PubMed Web of Science ®Google Scholar
• Raposo, G., & Stoorvogel, W. (2013). Extracellular vesicles: Exosomes, microvesicles, and friends. The Journal of Cell Biology, 200(4), 373–383. https://doi.org/10.1083/jcb.201211138
   PubMed Web of Science ®Google Scholar
• Rautureau, G. J. P., Day, C. L., & Hinds, M. G. (2010). Intrinsically disordered proteins in Bcl-2 regulated apoptosis. International Journal of Molecular Sciences, 11(4), 1808–1824. https://doi.org/10.3390/ijms11041808
   PubMed Web of Science ®Google Scholar
• Raymond, A. D., Campbell-Sims, T. C., Khan, M., Lang, M., Huang, M. B., Bond, V. C., & Powell, M. D. (2011). HIV Type 1 Nef is released from infected cells in CD45(+) microvesicles and is present in the plasma of HIV-infected individuals. AIDS Research and Human Retroviruses, 27(2), 167–178. https://doi.org/10.1089/aid.2009.0170
   PubMed Web of Science ®Google Scholar
• Ren, X., Kloer, D. P., Kim, Y. C., Ghirlando, R., Saidi, L. F., Hummer, G., & Hurley, J. H. (2009). Hybrid structural model of the complete human ESCRT-0 complex. Structure, 17(3), 406–416. https://doi.org/10.1016/j.str.2009.01.012
   PubMed Web of Science ®Google Scholar
• Reyes-Ruiz, J. M., Osuna-Ramos, J. F., De Jesús-González, L. A., Hurtado-Monzón, A. M., Farfan-Morales, C. N., Cervantes-Salazar, M., Bolaños, J., Cigarroa-Mayorga, O. E., Martín-Martínez, E. S., Medina, F., Fragoso-Soriano, R. J., Chávez-Munguía, B., Salas-Benito, J. S., & del Angel, R. M. (2019). Isolation and characterization of exosomes released from mosquito cells infected with dengue virus. Virus Research, 266, 1–14. https://doi.org/10.1016/j.virusres.2019.03.015
   PubMed Web of Science ®Google Scholar
• Rider, M. A., Hurwitz, S. N., & Meckes, D. G. Jr.(2016). ExtraPEG: A polyethylene glycol-based method for enrichment of extracellular vesicles. Scientific Reports, 6(1), 23978. https://doi.org/10.1038/srep23978
   PubMed Web of Science ®Google Scholar
• Roberts, G. S., Kozak, D., Anderson, W., Broom, M. F., Vogel, R., & Trau, M. (2010). Tunable nano/micropores for particle detection and discrimination: Scanning ion occlusion spectroscopy. Small, 6(23), 2653–2658. https://doi.org/10.1002/smll.201001129
   PubMed Web of Science ®Google Scholar
• Rodrigues, M., Fan, J., Lyon, C., Wan, M., & Hu, Y. (2018). Role of extracellular vesicles in viral and bacterial infections: Pathogenesis, diagnostics, and therapeutics. Theranostics, 8(10), 2709–2721. https://doi.org/10.7150/thno.20576
   PubMed Web of Science ®Google Scholar
• Romero, P., Obradovic, Z., Li, X., Garner, E. C., Brown, C. J., & Dunker, A. K. (2001). Sequence complexity of disordered protein. Proteins: Structure, Function, and Genetics, 42(1), 38–48. https://doi.org/10.1002/1097-0134(20010101)42:1<38::AID-PROT50>3.0.CO;2-3
   PubMed Web of Science ®Google Scholar
• Rozmyslowicz, T., Majka, M., Kijowski, J., Murphy, S. L., Conover, D. O., Poncz, M., Ratajczak, J., Gaulton, G. N., & Ratajczak, M. Z. (2003). Platelet- and megakaryocyte-derived microparticles transfer CXCR4 receptor to CXCR4-null cells and make them susceptible to infection by X4-HIV. AIDS (London, England), 17(1), 33–42. https://doi.org/10.1097/00002030-200301030-00006
   PubMed Web of Science ®Google Scholar
• Rust, M. J., Bates, M., & Zhuang, X. (2006). Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nature Methods, 3(10), 793–795. https://doi.org/10.1038/nmeth929
   PubMed Web of Science ®Google Scholar
• Sadeghipour, S., & Mathias, R. A. (2017). Herpesviruses hijack host exosomes for viral pathogenesis. Seminars in Cell & Developmental Biology, 67, 91–100. https://doi.org/10.1016/j.semcdb.2017.03.005
   PubMed Web of Science ®Google Scholar
• Sadler, A. J., & Williams, B. R. (2008). Interferon-inducible antiviral effectors. Nature Reviews Immunology, 8(7), 559–568. https://doi.org/10.1038/nri2314
   PubMed Web of Science ®Google Scholar
• Santiana, M., Ghosh, S., Ho, B. A., Rajasekaran, V., Du, W.-L., Mutsafi, Y., De Jésus-Diaz, D. A., Sosnovtsev, S. V., Levenson, E. A., Parra, G. I., Takvorian, P. M., Cali, A., Bleck, C., Vlasova, A. N., Saif, L. J., Patton, J. T., Lopalco, P., Corcelli, A., Green, K. Y., & Altan-Bonnet, N. (2018). Vesicle-cloaked virus clusters are optimal units for inter-organismal viral transmission. Cell Host & Microbe, 24(2), 208–220. https://doi.org/10.1016/j.chom.2018.07.006
   PubMed Web of Science ®Google Scholar
• Schad, E., Tompa, P., & Hegyi, H. (2011). The relationship between proteome size, structural disorder and organism complexity. Genome Biology, 12(12), R120. https://doi.org/10.1186/gb-2011-12-12-r120
   PubMed Web of Science ®Google Scholar
• Schoggins, J. W., & Rice, C. M. (2011). Interferon-stimulated genes and their antiviral effector functions. Current Opinion in Virology, 1(6), 519–525. https://doi.org/10.1016/j.coviro.2011.10.008
   PubMed Web of Science ®Google Scholar
• Schoneberg, J., Lee, I. H., Iwasa, J. H., & Hurley, J. H. (2017). Reverse-topology membrane scission by the ESCRT proteins. Nature Reviews Molecular Cell Biology, 18(1), 5–17. https://doi.org/10.1038/nrm.2016.121
   PubMed Web of Science ®Google Scholar
• Schorey, J. S., & Bhatnagar, S. (2008). Exosome function: From tumor immunology to pathogen biology. Traffic, 9(6), 871–881. https://doi.org/10.1111/j.1600-0854.2008.00734.x
   PubMed Web of Science ®Google Scholar
• Schwartz, Y. S., Dolganova, O. M., Rudina, M. I., Pyshnaya, I. A., & Bgatova, N. P. (2018). Influence of apoptotic bodies and apoptotic microvesicles on NO production in macrophages. Bulletin of Experimental Biology and Medicine, 165(4), 453–456. https://doi.org/10.1007/s10517-018-4192-9
   PubMed Web of Science ®Google Scholar
• Sharp, T. M., & Estes, M. K. (2010). An inside job: Subversion of the host secretory pathway by intestinal pathogens. Current Opinion in Infectious Diseases, 23(5), 464–469. https://doi.org/10.1097/QCO.0b013e32833dcebd
   PubMed Web of Science ®Google Scholar
• Shepard, C. W., Finelli, L., & Alter, M. J. (2005). Global epidemiology of hepatitis C virus infection. Lancet Infectious Diseases, 5(9), 558–567. https://doi.org/10.1016/S1473-3099(05)70216-4
   PubMed Web of Science ®Google Scholar
• Shimizu, K., & Toh, H. (2009). Interaction between intrinsically disordered proteins frequently occurs in a human protein-protein interaction network. Journal of Molecular Biology, 392(5), 1253–1265. https://doi.org/10.1016/j.jmb.2009.07.088
   PubMed Web of Science ®Google Scholar
• Shrivastava, S., Devhare, P., Sujijantarat, N., Steele, R., Kwon, Y. C., Ray, R., & Ray, R. B. (2016). Knockdown of autophagy inhibits infectious hepatitis C virus release by the exosomal pathway. Journal of Virology, 90(3), 1387–1396. https://doi.org/10.1128/JVI.02383-15
   PubMed Web of Science ®Google Scholar
• Silveira, G. F., Meyer, F., Delfraro, A., Mosimann, A. L. P., Coluchi, N., Vasquez, C., Probst, C. M., Bafica, A., Bordignon, J., & dos Santos, C. N. D. (2011). Dengue virus type 3 isolated from a fatal case with visceral complications induces enhanced proinflammatory responses and apoptosis of human dendritic cells. Journal of Virology, 85(11), 5374–5383. https://doi.org/10.1128/JVI.01915-10
   PubMed Web of Science ®Google Scholar
• Singh, V. V., Kerur, N., Bottero, V., Dutta, S., Chakraborty, S., Ansari, M. A., Paudel, N., Chikoti, L., & Chandran, B. (2013). Kaposi’s sarcoma-associated herpesvirus latency in endothelial and B cells activates gamma interferon-inducible protein 16-mediated inflammasomes. Journal of Virology, 87(8), 4417–4431. https://doi.org/10.1128/JVI.03282-12
   PubMed Web of Science ®Google Scholar
• Sinigaglia, L., Gracias, S., Décembre, E., Fritz, M., Bruni, D., Smith, N., Herbeuval, J.-P., Martin, A., Dreux, M., Tangy, F., & Jouvenet, N. (2018). Immature particles and capsid-free viral RNA produced by Yellow fever virus-infected cells stimulate plasmacytoid dendritic cells to secrete interferons. Scientific Reports, 8(1), 10889. https://doi.org/10.1038/s41598-018-29235-7
   PubMedGoogle Scholar
• Soderberg-Naucler, C., & Nelson, J. Y. (1999). Human cytomegalovirus latency and reactivation: A delicate balance between the virus and its host’s immune system. Intervirology, 42(5–6), 314–321. https://doi.org/10.1159/000053966
   PubMed Web of Science ®Google Scholar
• Sokolova, V., Ludwig, A.-K., Hornung, S., Rotan, O., Horn, P. A., Epple, M., & Giebel, B. (2011). Characterisation of exosomes derived from human cells by nanoparticle tracking analysis and scanning electron microscopy. Colloids and Surfaces B: Biointerfaces, 87(1), 146–150. https://doi.org/10.1016/j.colsurfb.2011.05.013
   PubMed Web of Science ®Google Scholar
• Spidel, J. L., Craven, R. C., Wilson, C. B., Patnaik, A., Wang, H., Mansky, L. M., & Wills, J. W. (2004). Lysines close to the Rous sarcoma virus late domain critical for budding. Journal of Virology, 78(19), 10606–10616. https://doi.org/10.1128/JVI.78.19.10606-10616.2004
   PubMed Web of Science ®Google Scholar
• Staras, S. A., Dollard, S. C., Radford, K. W., Flanders, W. D., Pass, R. F., & Cannon, M. J. (2006). Seroprevalence of cytomegalovirus infection in the United States, 1988–1994. Clinical Infectious Diseases, 43(9), 1143–1151. https://doi.org/10.1086/508173
   PubMed Web of Science ®Google Scholar
• Steen, H. B. (2004). Flow cytometer for measurement of the light scattering of viral and other submicroscopic particles. Cytometry A, 57A(2), 94–99. https://doi.org/10.1002/cyto.a.10115
   Web of Science ®Google Scholar
• Strack, B., Calistri, A., Craig, S., Popova, E., & Gottlinger, H. G. (2003). AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell, 114(6), 689–699. https://doi.org/10.1016/S0092-8674(03)00653-6
   PubMed Web of Science ®Google Scholar
• Straface, G., Selmin, A., Zanardo, V., De Santis, M., Ercoli, A., & Scambia, G. (2012). Herpes simplex virus infection in pregnancy. Infectious Diseases in Obstetrics and Gynecology, 2012, 1–6. https://doi.org/10.1155/2012/385697
   Google Scholar
• Stuermer, C. A., Lang, D. M., Kirsch, F., Wiechers, M., Deininger, S. O., & Plattner, H. (2001). Glycosylphosphatidyl inositol-anchored proteins and fyn kinase assemble in noncaveolar plasma membrane microdomains defined by reggie-1 and -2. Molecular Biology of the Cell, 12(10), 3031–3045. https://doi.org/10.1091/mbc.12.10.3031
   PubMed Web of Science ®Google Scholar
• Szklarczyk, D., Franceschini, A., Kuhn, M., Simonovic, M., Roth, A., Minguez, P., Doerks, T., Stark, M., Muller, J., Bork, P., Jensen, L. J., & Mering, C. v. (2011). The STRING database in 2011: Functional interaction networks of proteins, globally integrated and scored. Nucleic Acids Research, 39(Database issue), D561–568. https://doi.org/10.1093/nar/gkq973
   PubMed Web of Science ®Google Scholar
• Tandon, R., AuCoin, D. P., & Mocarski, E. S. (2009). Human cytomegalovirus exploits ESCRT machinery in the process of virion maturation. Journal of Virology, 83(20), 10797–10807. https://doi.org/10.1128/JVI.01093-09
   PubMed Web of Science ®Google Scholar
• Tatischeff, I., Larquet, E., Falcón-Pérez, J. M., Turpin, P.-Y., & Kruglik, S. G. (2012). Fast characterisation of cell-derived extracellular vesicles by nanoparticles tracking analysis, cryo-electron microscopy, and Raman tweezers microspectroscopy. Journal of Extracellular Vesicles, 1(1), 19179. https://doi.org/10.3402/jev.v1i0.19179
   PubMedGoogle Scholar
• Tavernarakis, N., Driscoll, M., & Kyrpides, N. C. (1999). The SPFH domain: Implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins. Trends in Biochemical Sciences, 24(11), 425–427. https://doi.org/10.1016/S0968-0004(99)01467-X
   PubMed Web of Science ®Google Scholar
• Taylor, D. D., & Gercel-Taylor, C. (2011). Exosomes/microvesicles: Mediators of cancer-associated immunosuppressive microenvironments. Seminars in Immunopathology, 33(5), 441–454. https://doi.org/10.1007/s00281-010-0234-8
   PubMed Web of Science ®Google Scholar
• Teijaro, J. R. (2016). Type I interferons in viral control and immune regulation. Current Opinion in Virology, 16, 31–40. https://doi.org/10.1016/j.coviro.2016.01.001
   PubMed Web of Science ®Google Scholar
• Temme, S., Eis-Hubinger, A. M., McLellan, A. D., & Koch, N. (2010). The herpes simplex virus-1 encoded glycoprotein B diverts HLA-DR into the exosome pathway. The Journal of Immunology, 184(1), 236–243. https://doi.org/10.4049/jimmunol.0902192
   PubMed Web of Science ®Google Scholar
• Teow, S. Y., Liew, K., Khoo, A. S., & Peh, S. C. (2017). Pathogenic role of exosomes in Epstein-Barr virus (EBV): Associated cancers. International Journal of Biological Sciences, 13(10), 1276–1286. https://doi.org/10.7150/ijbs.19531
   PubMed Web of Science ®Google Scholar
• Théry, C., Amigorena, S., Raposo, G., & Clayton, A. (2006). Isolation and characterization of exosomes from cell culture supernatants and biological fluids. Current Protocols in Cell Biology, 30(1), 22–21.
   Google Scholar
• Théry, C., Ostrowski, M., & Segura, E. (2009). Membrane vesicles as conveyors of immune responses. Nature Reviews Immunology, 9(8), 581–593. https://doi.org/10.1038/nri2567
   PubMed Web of Science ®Google Scholar
• Théry, C., Witwer, K. W., Aikawa, E., Alcaraz, M. J., Anderson, J. D., Andriantsitohaina, R., Antoniou, A., Arab, T., Archer, F., Atkin-Smith, G. K., Ayre, D. C., Bach, J.-M., Bachurski, D., Baharvand, H., Balaj, L., Baldacchino, S., Bauer, N. N., Baxter, A. A., Bebawy, M., … Zuba-Surma, E. K. (2018). Minimal information for studies of extracellular vesicles 2018 (MISEV2018): A position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines. Journal of Extracellular Vesicles, 7(1), 1535750. https://doi.org/10.1080/20013078.2018.1535750
   PubMed Web of Science ®Google Scholar
• Timmins, J., Schoehn, G., Ricard-Blum, S., Scianimanico, S., Vernet, T., Ruigrok, R. W., & Weissenhorn, W. (2003). Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4. Journal of Molecular Biology, 326(2), 493–502. https://doi.org/10.1016/S0022-2836(02)01406-7
   PubMed Web of Science ®Google Scholar
• Tokuriki, N., Oldfield, C. J., Uversky, V. N., Berezovsky, I. N., & Tawfik, D. S. (2009). Do viral proteins possess unique biophysical features? Trends in Biochemical Sciences, 34(2), 53–59. https://doi.org/10.1016/j.tibs.2008.10.009
   PubMed Web of Science ®Google Scholar
• Tompa, P. (2002). Intrinsically unstructured proteins. Trends in Biochemical Sciences, 27(10), 527–533. https://doi.org/10.1016/S0968-0004(02)02169-2
   PubMed Web of Science ®Google Scholar
• Tompa, P., Dosztanyi, Z., & Simon, I. (2006). Prevalent structural disorder in E. coli and S. cerevisiae proteomes. Journal of Proteome Research, 5(8), 1996–2000. https://doi.org/10.1021/pr0600881
   PubMed Web of Science ®Google Scholar
• Tompa, P., & Kalmar, L. (2010). Power law distribution defines structural disorder as a structural element directly linked with function. Journal of Molecular Biology, 403(3), 346–350. https://doi.org/10.1016/j.jmb.2010.07.044
   PubMed Web of Science ®Google Scholar
• Usami, Y., Popov, S., Popova, E., & GöTtlinger, H. G. (2008). Efficient and specific rescue of human immunodeficiency virus type 1 budding defects by a Nedd4-like ubiquitin ligase. Journal of Virology, 82(10), 4898–4907. https://doi.org/10.1128/JVI.02675-07
   PubMed Web of Science ®Google Scholar
• Uversky, V. N. (2002a). Natively unfolded proteins: A point where biology waits for physics. Protein Science, 11(4), 739–756. https://doi.org/10.1110/ps.4210102
   PubMed Web of Science ®Google Scholar
• Uversky, V. N. (2002b). What does it mean to be natively unfolded? European Journal of Biochemistry, 269(1), 2–12. https://doi.org/10.1046/j.0014-2956.2001.02649.x
   PubMedGoogle Scholar
• Uversky, V. N. (2003). Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: Which way to go? Cellular and Molecular Life Sciences, 60(9), 1852–1871. https://doi.org/10.1007/s00018-003-3096-6
   PubMed Web of Science ®Google Scholar
• Uversky, V. N. (2010). The mysterious unfoldome: Structureless, underappreciated, yet vital part of any given proteome. Journal of Biomedicine and Biotechnology, 2010, 1–14. https://doi.org/10.1155/2010/568068
   Google Scholar
• Uversky, V. N. (2013a). A decade and a half of protein intrinsic disorder: Biology still waits for physics. Protein Science, 22(6), 693–724. https://doi.org/10.1002/pro.2261
   PubMed Web of Science ®Google Scholar
• Uversky, V. N. (2013b). Intrinsic disorder-based protein interactions and their modulators. Current Pharmaceutical Design, 19(23), 4191–4213. https://doi.org/10.2174/1381612811319230005
   PubMed Web of Science ®Google Scholar
• Uversky, V. N. (2013c). Unusual biophysics of intrinsically disordered proteins. Biochimica et Biophysica Acta, 1834(5), 932–951. https://doi.org/10.1016/j.bbapap.2012.12.008
   PubMed Web of Science ®Google Scholar
• Uversky, V. N. (2015a). Functional roles of transiently and intrinsically disordered regions within proteins. FEBS Journal, 282(7), 1182–1189. https://doi.org/10.1111/febs.13202
   PubMed Web of Science ®Google Scholar
• Uversky, V. N. (2015b). The multifaceted roles of intrinsic disorder in protein complexes. FEBS Letters, 589(19 PartA), 2498–2506. https://doi.org/10.1016/j.febslet.2015.06.004
   PubMed Web of Science ®Google Scholar
• Uversky, V. N. (2016a). p53 proteoforms and intrinsic disorder: An illustration of the protein structure-function continuum concept. International Journal of Molecular Sciences, 17(11), E1874.
   PubMed Web of Science ®Google Scholar
• Uversky, V. N. (2016b). Paradoxes and wonders of intrinsic disorder: Complexity of simplicity. Intrinsically Disordered Proteins, 4(1), e1135015. https://doi.org/10.1080/21690707.2015.1135015
   PubMedGoogle Scholar
• Uversky, V. N. (2019). Protein intrinsic disorder and structure-function continuum. Progress in Molecular Biology and Translational Science, 166, 1–17. https://doi.org/10.1016/bs.pmbts.2019.05.003
   PubMed Web of Science ®Google Scholar
• Uversky, V. N., & Dunker, A. K. (2010). Understanding protein non-folding. Biochimica et Biophysica Acta, 1804(6), 1231–1264. https://doi.org/10.1016/j.bbapap.2010.01.017
   PubMed Web of Science ®Google Scholar
• Uversky, V. N., & Dunker, A. K. (2013). The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure. F1000 Biology Reports, 5, 1. https://doi.org/10.3410/B5-1
   PubMedGoogle Scholar
• Uversky, V. N., Gillespie, J. R., & Fink, A. L. (2000). Why are “natively unfolded” proteins unstructured under physiologic conditions? Proteins: Structure, Function, and Genetics, 41(3), 415–427. https://doi.org/10.1002/1097-0134(20001115)41:3<415::AID-PROT130>3.0.CO;2-7
   PubMed Web of Science ®Google Scholar
• Vacic, V., Uversky, V. N., Dunker, A. K., & Lonardi, S. (2007). Composition profiler: A tool for discovery and visualization of amino acid composition differences. BMC Bioinformatics, 8(1), 211. https://doi.org/10.1186/1471-2105-8-211
   PubMed Web of Science ®Google Scholar
• Valadi, H., Ekström, K., Bossios, A., Sjöstrand, M., Lee, J. J., & Lötvall, J. O. (2007). Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells. Nature Cell Biology, 9(6), 654–659. https://doi.org/10.1038/ncb1596
   PubMed Web of Science ®Google Scholar
• Valenzuela, M. M., Ferguson Bennit, H. R., Gonda, A., Diaz Osterman, C. J., Hibma, A., Khan, S., & Wall, N. R. (2015). Exosomes secreted from human cancer cell lines contain inhibitors of apoptosis (IAP). Cancer Microenvironment, 8(2), 65–73. https://doi.org/10.1007/s12307-015-0167-9
   PubMed Web of Science ®Google Scholar
• van der Lee, R., Buljan, M., Lang, B., Weatheritt, R. J., Daughdrill, G. W., Dunker, A. K., Fuxreiter, M., Gough, J., Gsponer, J., Jones, D. T., Kim, P. M., Kriwacki, R. W., Oldfield, C. J., Pappu, R. V., Tompa, P., Uversky, V. N., Wright, P. E., & Babu, M. M. (2014). Classification of intrinsically disordered regions and proteins. Chemical Reviews, 114(13), 6589–6631. https://doi.org/10.1021/cr400525m
   PubMed Web of Science ®Google Scholar
• Van Der Pol, E., Hoekstra, A. G., Sturk, A., Otto, C., Van Leeuwen, T. G., & Nieuwland, R. (2010). Optical and non‐optical methods for detection and characterization of microparticles and exosomes. Journal of Thrombosis and Haemostasis, 8(12), 2596–2607. https://doi.org/10.1111/j.1538-7836.2010.04074.x
   PubMed Web of Science ®Google Scholar
• van Niel, G., D’Angelo, G., & Raposo, G. (2018). Shedding light on the cell biology of extracellular vesicles. Nature Reviews Molecular Cell Biology, 19(4), 213–228. https://doi.org/10.1038/nrm.2017.125
   PubMed Web of Science ®Google Scholar
• VerPlank, L., Bouamr, F., LaGrassa, T. J., Agresta, B., Kikonyogo, A., Leis, J., & Carter, C. A. (2001). Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag). Proceedings of the National Academy of Sciences, 98(14), 7724–7729. https://doi.org/10.1073/pnas.131059198
   PubMed Web of Science ®Google Scholar
• Verweij, F. J., van Eijndhoven, M. A., Middeldorp, J., & Pegtel, D. M. (2013). Analysis of viral microRNA exchange via exosomes in vitro and in vivo. Methods in Molecular Biology (Clifton, NJ), 1024, 53–68. https://doi.org/10.1007/978-1-62703-453-1_5
   PubMedGoogle Scholar
• Vidal, M., Sainte-Marie, J., Philippot, J. R., & Bienvenue, A. (1989). Asymmetric distribution of phospholipids in the membrane of vesicles released during in vitro maturation of guinea pig reticulocytes: Evidence precluding a role for “aminophospholipid translocase”. Journal of Cellular Physiology, 140(3), 455–462. https://doi.org/10.1002/jcp.1041400308
   PubMed Web of Science ®Google Scholar
• Vidal, M. J., & Stahl, P. D. (1993). The small GTP-binding proteins Rab4 and ARF are associated with released exosomes during reticulocyte maturation. European Journal of Cell Biology, 60(2), 261–267.
   PubMed Web of Science ®Google Scholar
• Vidigal, J. A., & Ventura, A. (2015). The biological functions of miRNAs: Lessons from in vivo studies. Trends in Cell Biology, 25(3), 137–147. https://doi.org/10.1016/j.tcb.2014.11.004
   PubMed Web of Science ®Google Scholar
• Villarroya-Beltri, C., Baixauli, F., Mittelbrunn, M., Fernández-Delgado, I., Torralba, D., Moreno-Gonzalo, O., Baldanta, S., Enrich, C., Guerra, S., & Sánchez-Madrid, F. (2016). ISGylation controls exosome secretion by promoting lysosomal degradation of MVB proteins. Nature Communications, 7(1), 13588. https://doi.org/10.1038/ncomms13588
   PubMedGoogle Scholar
• Vlassov, A. V., Magdaleno, S., Setterquist, R., & Conrad, R. (2012). Exosomes: Current knowledge of their composition, biological functions, and diagnostic and therapeutic potentials. Biochimica et Biophysica Acta, 1820(7), 940–948. https://doi.org/10.1016/j.bbagen.2012.03.017
   PubMed Web of Science ®Google Scholar
• Vogel, R., Willmott, G., Kozak, D., Roberts, G. S., Anderson, W., Groenewegen, L., Glossop, B., Barnett, A., Turner, A., & Trau, M. (2011). Quantitative sizing of nano/microparticles with a tunable elastomeric pore sensor. Analytical Chemistry, 83(9), 3499–3506. https://doi.org/10.1021/ac200195n
   PubMed Web of Science ®Google Scholar
• Vora, A., Zhou, W., Londono-Renteria, B., Woodson, M., Sherman, M. B., Colpitts, T. M., Neelakanta, G., & Sultana, H. (2018). Arthropod EVs mediate dengue virus transmission through interaction with a tetraspanin domain containing glycoprotein Tsp29Fb. Proceedings of the National Academy of Sciences, 115(28), E6604–E6613. https://doi.org/10.1073/pnas.1720125115
   PubMed Web of Science ®Google Scholar
• Votteler, J., & Sundquist, W. I. (2013). Virus budding and the ESCRT pathway. Cell Host & Microbe, 14(3), 232–241. https://doi.org/10.1016/j.chom.2013.08.012
   PubMed Web of Science ®Google Scholar
• Walker, J. D., Maier, C. L., & Pober, J. S. (2009). Cytomegalovirus-infected human endothelial cells can stimulate allogeneic CD4+ memory T cells by releasing antigenic exosomes. The Journal of Immunology, 182(3), 1548–1559. https://doi.org/10.4049/jimmunol.182.3.1548
   PubMed Web of Science ®Google Scholar
• Walsh, I., Martin, A. J., Di Domenico, T., & Tosatto, S. C. (2012). ESpritz: Accurate and fast prediction of protein disorder. Bioinformatics, 28(4), 503–509. https://doi.org/10.1093/bioinformatics/btr682
   PubMed Web of Science ®Google Scholar
• Wang, A., Thurmond, S., Islas, L., Hui, K., & Hai, R. (2017). Zika virus genome biology and molecular pathogenesis. Emerging Microbes & Infections, 6(1), e13–e16. https://doi.org/10.1038/emi.2016.141
   PubMedGoogle Scholar
• Wang, Z., Wu, H-j., Fine, D., Schmulen, J., Hu, Y., Godin, B., Zhang, J. X. J., & Liu, X. (2013). Ciliated micropillars for the microfluidic-based isolation of nanoscale lipid vesicles. Lab on a Chip, 13(15), 2879–2882. https://doi.org/10.1039/c3lc41343h
   PubMed Web of Science ®Google Scholar
• Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F., & Jones, D. T. (2004). Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. Journal of Molecular Biology, 337(3), 635–645. https://doi.org/10.1016/j.jmb.2004.02.002
   PubMed Web of Science ®Google Scholar
• Waruiru, C., Slatter, M. A., Taylor, C., Ramesh, V., Flood, T. J., Abinun, M., Cant, A. J., & Gennery, A. R. (2007). Outcome of hematopoietic stem cell transplantation in severe combined immune deficiency with central nervous system viral infection. The Pediatric Infectious Disease Journal, 26(2), 129–133. https://doi.org/10.1097/01.inf.0000250621.46742.b5
   PubMed Web of Science ®Google Scholar
• Weidner, J. M., Jiang, D., Pan, X.-B., Chang, J., Block, T. M., & Guo, J.-T. (2010). Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms. Journal of Virology, 84(24), 12646–12657. https://doi.org/10.1128/JVI.01328-10
   PubMed Web of Science ®Google Scholar
• Weiss, E. R., Popova, E., Yamanaka, H., Kim, H. C., Huibregtse, J. M., & Gottlinger, H. (2010). Rescue of HIV-1 release by targeting widely divergent NEDD4-type ubiquitin ligases and isolated catalytic HECT domains to Gag. PLoS Pathogens, 6(9), e1001107. https://doi.org/10.1371/journal.ppat.1001107
   PubMed Web of Science ®Google Scholar
• Weiss, R. A. (1993). How does HIV cause AIDS? Science, 260(5112), 1273–1279. https://doi.org/10.1126/science.8493571
   PubMed Web of Science ®Google Scholar
• Williams, R. M., Obradovic, Z., Mathura, V., Braun, W., Garner, E. C., Young, J., … Dunker, A. K. (2001). The protein non-folding problem: Amino acid determinants of intrinsic order and disorder. Pac Symp Biocomput, 2001, 89–100.
   Google Scholar
• Witwer, K. W., Buzás, E. I., Bemis, L. T., Bora, A., Lässer, C., Lötvall, J., Nolte-‘T Hoen, E. N., Piper, M. G., Sivaraman, S., Skog, J., Théry, C., Wauben, M. H., & Hochberg, F. (2013). Standardization of sample collection, isolation and analysis methods in extracellular vesicle research. Journal of Extracellular Vesicles, 2(1), 20360. https://doi.org/10.3402/jev.v2i0.20360
   PubMedGoogle Scholar
• Witwer, K. W., & Thery, C. (2019). Extracellular vesicles or exosomes? On primacy, precision, and popularity influencing a choice of nomenclature. Journal of Extracellular Vesicles, 8(1), 1648167. https://doi.org/10.1080/20013078.2019.1648167
   PubMed Web of Science ®Google Scholar
• Wright, P. E., & Dyson, H. J. (1999). Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm. Journal of Molecular Biology, 293(2), 321–331. https://doi.org/10.1006/jmbi.1999.3110
   PubMed Web of Science ®Google Scholar
• Wu, Y. W., Mettling, C., Wu, S. R., Yu, C. Y., Perng, G. C., Lin, Y. S., & Lin, Y. L. (2016). Autophagy-associated dengue vesicles promote viral transmission avoiding antibody neutralization. Scientific Reports, 6(1), 32243. https://doi.org/10.1038/srep32243
   PubMedGoogle Scholar
• Wurdinger, T., Gatson, N. N., Balaj, L., Kaur, B., Breakefield, X. O., & Pegtel, D. M. (2012). Extracellular vesicles and their convergence with viral pathways. Advances in Virology, 2012, 1–12. https://doi.org/10.1155/2012/767694
   Google Scholar
• Xiao, F., Fofana, I., Heydmann, L., Barth, H., Soulier, E., Habersetzer, F., Doffoël, M., Bukh, J., Patel, A. H., Zeisel, M. B., & Baumert, T. F. (2014). Hepatitis C virus cell-cell transmission and resistance to direct-acting antiviral agents. PLoS Pathogens, 10(5), e1004128. https://doi.org/10.1371/journal.ppat.1004128
   PubMed Web of Science ®Google Scholar
• Xu, R., Greening, D. W., Rai, A., Ji, H., & Simpson, R. J. (2015). Highly-purified exosomes and shed microvesicles isolated from the human colon cancer cell line LIM1863 by sequential centrifugal ultrafiltration are biochemically and functionally distinct. Methods, 87, 11–25. https://doi.org/10.1016/j.ymeth.2015.04.008
   PubMed Web of Science ®Google Scholar
• Xue, B., Dunker, A. K., & Uversky, V. N. (2012). Orderly order in protein intrinsic disorder distribution: Disorder in 3500 proteomes from viruses and the three domains of life. Journal of Biomolecular Structure and Dynamics, 30(2), 137–149. https://doi.org/10.1080/07391102.2012.675145
   PubMed Web of Science ®Google Scholar
• Xue, B., Romero, P. R., Noutsou, M., Maurice, M. M., Rüdiger, S. G. D., William, A. M., Mizianty, M. J., Kurgan, L., Uversky, V. N., & Dunker, A. K. (2013). Stochastic machines as a colocalization mechanism for scaffold protein function. FEBS Letters, 587(11), 1587–1591. https://doi.org/10.1016/j.febslet.2013.04.006
   PubMed Web of Science ®Google Scholar
• Xue, B., Williams, R. W., Oldfield, C. J., Dunker, A. K., & Uversky, V. N. (2010). Archaic chaos: Intrinsically disordered proteins in Archaea. BMC Systems Biology, 4 (Suppl 1), S1.
   PubMed Web of Science ®Google Scholar
• Yakimchuk, K. (2015). Exosomes: Isolation and characterization methods and specific markers. Materials and Methods, 5, 1450. https://doi.org/10.13070/mm.en.5.1450
   Google Scholar
• Yamada, T., Inoshima, Y., Matsuda, T., & Ishiguro, N. (2012). Comparison of methods for isolating exosomes from bovine milk. Journal of Veterinary Medical Science, 74(11), 1523–1525. https://doi.org/10.1292/jvms.12-0032
   PubMed Web of Science ®Google Scholar
• Yáñez-Mó, M., Siljander, P. R.-M., Andreu, Z., Bedina Zavec, A., Borràs, F. E., Buzas, E. I., Buzas, K., Casal, E., Cappello, F., Carvalho, J., Colás, E., Cordeiro-da Silva, A., Fais, S., Falcon-Perez, J. M., Ghobrial, I. M., Giebel, B., Gimona, M., Graner, M., Gursel, I., … De Wever, O. (2015). Biological properties of extracellular vesicles and their physiological functions. Journal of Extracellular Vesicles, 4(1), 27066. https://doi.org/10.3402/jev.v4.27066
   PubMed Web of Science ®Google Scholar
• Yao, L., Dong, H., Zhu, H., Nelson, D., Liu, C., Lambiase, L., & Li, X. (2011). Identification of the IFITM3 gene as an inhibitor of hepatitis C viral translation in a stable STAT1 cell line. Journal of Viral Hepatitis, 18(10), e523–e529. https://doi.org/10.1111/j.1365-2893.2011.01452.x
   PubMed Web of Science ®Google Scholar
• Yasuda, J., Nakao, M., Kawaoka, Y., & Shida, H. (2003). Nedd4 regulates egress of Ebola virus-like particles from host cells. Journal of Virology, 77(18), 9987–9992. https://doi.org/10.1128/JVI.77.18.9987-9992.2003
   PubMed Web of Science ®Google Scholar
• Young, L. S., Yap, L. F., & Murray, P. G. (2016). Epstein-Barr virus: More than 50 years old and still providing surprises. Nature Reviews Cancer, 16(12), 789–802. https://doi.org/10.1038/nrc.2016.92
   PubMed Web of Science ®Google Scholar
• Yuana, Y., Oosterkamp, T., Bahatyrova, S., Ashcroft, B., Garcia Rodriguez, P., Bertina, R., & Osanto, S. (2010). Atomic force microscopy: A novel approach to the detection of nanosized blood microparticles. Journal of Thrombosis and Haemostasis, 8(2), 315–323. https://doi.org/10.1111/j.1538-7836.2009.03654.x
   PubMed Web of Science ®Google Scholar
• Zhadina, M., McClure, M. O., Johnson, M. C., & Bieniasz, P. D. (2007). Ubiquitin-dependent virus particle budding without viral protein ubiquitination. Proceedings of the National Academy of Sciences, 104(50), 20031–20036. https://doi.org/10.1073/pnas.0708002104
   PubMed Web of Science ®Google Scholar
• Zhang, H., Freitas, D., Kim, H. S., Fabijanic, K., Li, Z., Chen, H., Mark, M. T., Molina, H., Martin, A. B., Bojmar, L., Fang, J., Rampersaud, S., Hoshino, A., Matei, I., Kenific, C. M., Nakajima, M., Mutvei, A. P., Sansone, P., Buehring, W., … Lyden, D. (2018). Identification of distinct nanoparticles and subsets of extracellular vesicles by asymmetric flow field-flow fractionation. Nature Cell Biology, 20(3), 332–343. https://doi.org/10.1038/s41556-018-0040-4
   PubMed Web of Science ®Google Scholar
• Zhang, T., Faraggi, E., Li, Z., & Zhou, Y. (2013). Intrinsically semi-disordered state and its role in induced folding and protein aggregation. Cell Biochemistry and Biophysics, 67(3), 1193–1205. https://doi.org/10.1007/s12013-013-9638-0
   PubMed Web of Science ®Google Scholar
• Zhang, Z., Yu, X., Zhou, Z., Li, B., Peng, J., Wu, X., Luo, X., & Yang, L. (2019). LMP1-positive extracellular vesicles promote radioresistance in nasopharyngeal carcinoma cells through P38 MAPK signaling. Cancer Medicine, 8(13), 6082–6094. https://doi.org/10.1002/cam4.2506
   PubMed Web of Science ®Google Scholar
• Zhao, M., Nanbo, A., Sun, L., & Lin, Z. (2019). Extracellular vesicles in Epstein-Barr virus’ life cycle and pathogenesis. Microorganisms, 7(2), 48. https://doi.org/10.3390/microorganisms7020048
   Web of Science ®Google Scholar
• Zhou, W., Woodson, M., Neupane, B., Bai, F., Sherman, M. B., Choi, K. H., Neelakanta, G., & Sultana, H. (2018). Exosomes serve as novel modes of tick-borne flavivirus transmission from arthropod to human cells and facilitates dissemination of viral RNA and proteins to the vertebrate neuronal cells. PLOS Pathogens, 14(1), e1006764. https://doi.org/10.1371/journal.ppat.1006764
   PubMed Web of Science ®Google Scholar
• Zhou, W., Woodson, M., Sherman, M. B., Neelakanta, G., & Sultana, H. (2019). Exosomes mediate Zika virus transmission through SMPD3 neutral Sphingomyelinase in cortical neurons. Emerging Microbes & Infections, 8(1), 307–326. https://doi.org/10.1080/22221751.2019.1578188
   PubMed Web of Science ®Google Scholar
• Zhu, X., He, Z., Yuan, J., Wen, W., Huang, X., Hu, Y., Lin, C., Pan, J., Li, R., Deng, H., Liao, S., Zhou, R., Wu, J., Li, J., & Li, M. (2015). IFITM3‐containing exosome as a novel mediator for anti‐viral response in dengue virus infection. Cellular Microbiology, 17(1), 105–118. https://doi.org/10.1111/cmi.12339
   PubMed Web of Science ®Google Scholar