Molecular Basis for Pathogenicity of Human Coronaviruses

References

• Lu R, Zhao X, Li J, et al. Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. Lancet. 2020;395(10224):565–574. doi:10.1016/S0140-6736(20)30251-832007145
   PubMed Web of Science ®Google Scholar
• Wrapp D, Wang N, Corbett KS, et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science. 2020;367(6483):1260–1263. doi:10.1126/science.abb250732075877
   PubMed Web of Science ®Google Scholar
• Ceraolo C, Giorgi FM. Genomic variance of the 2019-nCoV coronavirus. J Med Virol. 2020;92(5):522–528. doi:10.1002/jmv.2570032027036
   PubMed Web of Science ®Google Scholar
• Andersen KG, Rambaut A, Lipkin WI, Holmes EC, Garry RF. The proximal origin of SARS-CoV-2. Nat Med. 2020;26(4):450–452. doi:10.1038/s41591-020-0820-932284615
   PubMed Web of Science ®Google Scholar
• Ceccarelli M, Berretta M, Venanzi Rullo E, Nunnari G, Cacopardo B. Differences and similarities between severe acute respiratory syndrome (SARS)-coronavirus (CoV) and SARS-CoV-2. Would a rose by another name smell as sweet? Eur Rev Med Pharmacol Sci. 2020;24(5):2781–2783. doi:10.26355/eurrev_202003_2055132196628
   PubMed Web of Science ®Google Scholar
• Lan J, Ge J, Yu J, et al. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature. 2020;581(7807):215–220. doi:10.1038/s41586-020-2180-532225176
   PubMed Web of Science ®Google Scholar
• van Doremalen N, Bushmaker T, Morris DH, et al. Aerosol and surface stability of SARS-CoV-2 as compared with SARS-CoV-1. N Engl J Med. 2020;382(16):1564–1567. doi:10.1056/NEJMc200497332182409
   PubMed Web of Science ®Google Scholar
• Wang N, Shi X, Jiang L, et al. Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4. Cell Res. 2013;23(8):986–993. doi:10.1038/cr.2013.9223835475
   PubMed Web of Science ®Google Scholar
• Yuan P, Yang Z, Song H, et al. Three main inducers of alphacoronavirus infection of enterocytes: sialic acid, proteases, and low pH. Intervirology. 2018;61(2):53–63. doi:10.1159/00049242430176660
   PubMed Web of Science ®Google Scholar
• Cui J, Li F, Shi ZL. Origin and evolution of pathogenic coronaviruses. Nat Rev Microbiol. 2019;17(3):181–182. doi:10.1038/s41579-018-0118-930531947
   PubMed Web of Science ®Google Scholar
• Li F, Goff SP. Receptor recognition mechanisms of coronaviruses: a decade of structural studies. J Virol. 2015;89(4):1954–1964. doi:10.1128/JVI.02615-1425428871
   PubMed Web of Science ®Google Scholar
• Tortorici MA, Walls AC, Lang Y, et al. Structural basis for human coronavirus attachment to sialic acid receptors. Nat Struct Mol Biol. 2019;26(6):481–489. doi:10.1038/s41594-019-0233-y31160783
   PubMed Web of Science ®Google Scholar
• Widagdo W, Sooksawasdi S, Ayudhya N, Hundie GB, Haagmans BL. Host determinants of MERS-CoV transmission and pathogenesis. Viruses. 2019;11(280):2–14. doi:10.3390/v11030280
   Web of Science ®Google Scholar
• Song Z, Xu Y, Bao L, et al. From SARS to MERS, thrusting coronaviruses into the spotlight. Viruses. 2019;11(59):1–29. doi:10.3390/v11010059
   Web of Science ®Google Scholar
• Du L, He Y, Zhou Y, Liu S, Zheng BJ, Jiang S. The spike protein of SARS-CoV — a target for vaccine and therapeutic development. Nat Rev Microbiol. 2009;7(3):226–236. doi:10.1038/nrmicro209019198616
   PubMed Web of Science ®Google Scholar
• Kruse RL. Therapeutic strategies in an outbreak scenario to treat the novel coronavirus originating in Wuhan, China [version 2; peer review: 2 approved]. F1000Research. 2020;9(72):1–14. doi:10.12688/f1000research.22211.2
   Google Scholar
• Jia HP, Look DC, Shi L, et al. ACE2 receptor expression and severe acute respiratory syndrome coronavirus infection depend on differentiation of human airway epithelia. J Virol. 2005;79(23):14614–14621. doi:10.1128/JVI.79.23.14614-14621.200516282461
   PubMed Web of Science ®Google Scholar
• Li W, Hulswit RJG, Widjaja L, et al. Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein. PNAS. 2017;114(40):E8508–E8517. doi:10.1073/pnas.171259211428923942
   PubMed Web of Science ®Google Scholar
• Qing E, Hantak M, Perlman S, Gallagher T, Denison MR. Distinct roles for sialoside and protein receptors in coronavirus infection. mBio. 2020;11(1):e02764–19. doi:10.1128/mBio.02764-1932047128
   PubMed Web of Science ®Google Scholar
• Zhou P, Yang XL, Wang XG, et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020;579(7798):270–273. doi:10.1038/s41586-020-2012-732015507
   PubMed Web of Science ®Google Scholar
• Fehr AR, Perlman S. Coronaviruses: an overview of their replication and pathogenesis. Methods Mol Biol. 2015;1282:1–23.25720466
   PubMedGoogle Scholar
• Song EW, Gui M, Wang X, Xiang Y, Heise MT. Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. PLoS Pathog. 2018;14(8):e1007236. doi:10.1371/journal.ppat.100723630102747
   PubMed Web of Science ®Google Scholar
• Wan Y, Shang J, Graham R, Baric RS, Li F, Gallagher T. Receptor recognition by novel coronavirus from Wuhan: an analysis based on decade-long structural studies of SARS. J Virol. 2020;94(7). doi:10.1128/JVI.00127-20
   Web of Science ®Google Scholar
• Tikellis C, Thomas MC. Angiotensin-converting enzyme 2 (ACE2) is a key modulator of the renin angiotensin systemin health and disease. Int J Pept. 2012;2012:1–8. doi:10.1155/2012/256294
   Google Scholar
• Cao Y, Li L, Feng Z, et al. Comparative genetic analysis of the novel coronavirus (2019-nCoV/SARS-CoV-2) receptor ACE2 in different populations. Cell Disc. 2020;6(11):1–4.
   Google Scholar
• Widagdo W, Okba NMA, Li W, et al. Species-specific colocalization of Middle East respiratory syndrome coronavirus attachment and entry receptors. J Virol. 2019;93(16):e00107–19. doi:10.1128/JVI.00107-1931167913
   PubMed Web of Science ®Google Scholar
• Park YJ, Walls AC, Wang Z, et al. Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors. Nat Struct Mol Biol. 2019;26(12):1151–1157. doi:10.1038/s41594-019-0334-731792450
   PubMed Web of Science ®Google Scholar
• Schwegmann-Webels C, Herrler G. Sialic acids as receptor determinants for coronaviruses. Glycoconj J. 2006;23(1–2):51–58. doi:10.1007/s10719-006-5437-916575522
   PubMed Web of Science ®Google Scholar
• Wielgat P, Trofimiuk E, Czarnomysy R, Holownia A, Braszko JJ. Sialylation pattern in lung epithelial cell line and siglecs expression in monocytic THP-1 cells as cellular indicators of cigarette smoke-induced pathology in vitro. Exp Lung Res. 2018;44(3):167–177. doi:10.1080/01902148.2018.146195929781747
   PubMed Web of Science ®Google Scholar
• Wu C, Liu Y, Yang Y, et al. Analysis of therapeutic targets for SARS-CoV-2 and discovery of potential drugs by computational methods. Acta Pharm Sin B. 2020. doi:doi.10.1016/j.apsb.2020.02.008
   Web of Science ®Google Scholar
• Vankadari N, Wilce JA. Emerging WuHan (COVID-19) coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26. Emerg Microbes Infect. 2020;9(1):601–604. doi:10.1080/22221751.2020.173956532178593
   PubMed Web of Science ®Google Scholar
• Hoffmann M, Kleine-Weber H, Schroeder S, et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell. 2020;181(2):271–280. doi:10.1016/j.cell.2020.02.05232142651
   PubMed Web of Science ®Google Scholar
• Kim D, Lee JY, Yang JS, Kim JW, Kim VN, Chang H. The architecture of SARS-CoV-2 transcriptome. Cell. 2020;181(4):914–921. doi:10.1016/j.cell.2020.04.01132330414
   PubMed Web of Science ®Google Scholar
• Mercatelli D, Giorgi FM. Geographic and Genomic Distribution of SARS-Cov-2 Mutations. Preprints; 2020:2020040529. doi:10.20944/preprints202004.0529.v1
   Google Scholar
• Yang HC, Chen CH, Wang JH, et al. Genomic, geographic and temporal distributions of SARS-CoV-2 mutations. bioRxiv. 2020. doi:10.1101/2020.04.22.055863.
   Google Scholar
• Letko M, Marzi A, Munster V. Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses. Nat Microbiol. 2020;5(4):562–569. doi:10.1038/s41564-020-0688-y32094589
   PubMed Web of Science ®Google Scholar
• Wasik BR, Barnard KN, Ossiboff RJ, et al. Distribution of O-acetylated sialic acids among target host tissues for influenza virus. mSphere. 2017;2(5):e00379–16. doi:10.1128/mSphere.00379-16
   Web of Science ®Google Scholar
• Nicholls JM, Bourne AJ, Chen H, Guan Y, Peiris JSM. Sialic acid receptor detection in the human respiratory tract: evidence for widespread distribution of potential binding sites for human and avian influenza viruses. Respir Res. 2007;8(73):1–10. doi:10.1186/1465-9921-8-7317207287
   PubMed Web of Science ®Google Scholar
• Neumann G, Shinya K, Kawaoka Y. Molecular pathogenesis of H5N1 influenza virus infections. Antivir Ther. 2007;12(4 Pt B):617–626.17944269
   PubMed Web of Science ®Google Scholar
• Neumann G, Chen H, Gao GF, Shu Y, Kawaoka Y. H5N1 influenza viruses: outbreaks and biological properties. Cell Res. 2010;20(1):51–61. doi:10.1038/cr.2009.12419884910
   PubMed Web of Science ®Google Scholar
• Li YH, Hu CY, Wu NP, Yao HP, Li LJ. Molecular characteristics, functions, and related pathogenicity of MERS-CoV proteins. Eng. 2019;5(5):940–947. doi:10.1016/j.eng.2018.11.035
   Web of Science ®Google Scholar
• HU W. Molecular features of highly pathogenic avian and human H5N1 influenza a viruses in Asia. Comput Mol Biosci. 2012;2(02):45–59. doi:10.4236/cmb.2012.22005
   Google Scholar
• Hanisch F, Weidemann W, Großmann M, et al. Sialylation and muscle performance: sialic acid is a marker of muscle ageing. PLoS One. 2013;8(12):e80520. doi:10.1371/journal.pone.008052024349002
   PubMed Web of Science ®Google Scholar
• Fantini J, Di Scala C, Chahinian H, Yahi N. Structural and molecular modelling studies reveal a new mechanism of action of chloroquine and hydroxychloroquine against SARS-CoV-2 infection. Int J Antimicrob Agents. 2020;55(5):105960. doi:10.1016/j.ijantimicag.2020.10596032251731
   PubMed Web of Science ®Google Scholar
• Zhao X, Guo F, Comunale MA, et al. Inhibition of endoplasmic reticulum-resident glucosidases impairs severe acute respiratory syndrome coronavirus and human coronavirus NL63 spike protein-mediated entry by altering the glycan processing of angiotensin I-converting enzyme 2. Antimicrob Agents Chemother. 2015;59(1):206–216. doi:10.1128/AAC.03999-1425348530
   PubMed Web of Science ®Google Scholar
• Dutta A, Huang C-T, Lin C-Y, et al. Sterilizing immunity to influenza virus infection requires local antigen-specific T cell response in the lungs. Sci Rep. 2016;6(1):1–14. doi:10.1038/srep3297328442746
   PubMed Web of Science ®Google Scholar
• Schoeman D, Fielding BC. Coronavirus envelope protein: current knowledge. Virol J. 2019;16(69):2–22. doi:10.1186/s12985-019-1182-030611287
   PubMed Web of Science ®Google Scholar
• He Y, Zhou Y, Liu S, et al. Receptor-binding domain of SARS-CoV spike protein induces highly potent neutralizing antibodies: implication for developing subunit vaccine. Biochem Biophys Res Commun. 2004;324(2):773–781. doi:10.1016/j.bbrc.2004.09.10615474494
   PubMed Web of Science ®Google Scholar
• He Y, Li J, Li W, Lustigman S, Farzan M, Jiang S. Cross-neutralization of human and palm civet severe acute respiratory syndrome coronaviruses by antibodies targeting the receptor-binding domain of spike protein. J Immunol. 2006;176(10):c6085‐92. doi:10.4049/jimmunol.176.10.6085
   Web of Science ®Google Scholar
• Zhao J, Zhao J, Mangalam AK, et al. Airway memory CD4(+) T cells mediate protective immunity against emerging respiratory coronaviruses. Immunity. 2016;44(6):1379–1391. doi:10.1016/j.immuni.2016.05.00627287409
   PubMed Web of Science ®Google Scholar
• Tai W, Wang Y, Fett CA, et al. Recombinant receptor-binding domains of multiple middle east respiratory syndrome coronaviruses (MERS-CoVs) induce cross-neutralizing antibodies against divergent human and camel MERS-CoVs and antibody escape mutants. J Virol. 2016;91(1):e01651–16. doi:10.1128/JVI.01651-1627795425
   PubMed Web of Science ®Google Scholar