References
- Dhama K, Sharun K, Tiwari R, Dadar M, Malik YS, Singh KP, Chaicumpa W. COVID-19, an emerging coronavirus infection: advances and prospects in designing and developing vaccines, immunotherapeutics, and therapeutics. Hum Vaccin Immunother. 2020:1–7. doi:https://doi.org/10.1080/21645515.2020.1735227.
- Bai Y, Yao L, Wei T, Tian F, Jin DY, Chen L, Wang M. Presumed asymptomatic carrier transmission of COVID-19. JAMA. 2020. doi:https://doi.org/10.1001/jama.2020.2565.
- Cunningham AC, Goh HP, Koh D. Treatment of COVID-19: old tricks for new challenges. Crit Care. 2020;24(1):91. doi:https://doi.org/10.1186/s13054-020-2818-6.
- Zheng YY, Ma YT, Zhang JY, Xie X. COVID-19 and the cardiovascular system. Nat Rev Cardiol. 2020;17(5):259–60. doi:https://doi.org/10.1038/s41569-020-0360-5.
- Pang J, Wang MX, Ang IYH, Tan SHX, Lewis RF, Chen JI, Gutierrez RA, Gwee SXW, Chua PEY, Yang Q, et al. Potential rapid diagnostics, vaccine and therapeutics for 2019 novel coronavirus (2019-nCoV): a systematic review. J Clin Med. 2020;9(3):pii: E623. doi:https://doi.org/10.3390/jcm9030623.
- Katzelnick LC, Gresh L, Halloran ME, Mercado JC, Kuan G, Gordon A. Antibody-dependent enhancement of severe dengue disease in humans. Science. 2017;358(6365):929–32. doi:https://doi.org/10.1126/science.aan6836.
- Khandia R, Munjal A, Dhama K, Karthik K, Tiwari R, Malik YS, Singh RK, Chaicumpa W. Modulation of dengue/zika virus pathogenicity by antibody-dependent enhancement and strategies to protect against enhancement in zika virus infection. Front Immunol. 2018;9:597. doi:https://doi.org/10.3389/fimmu.2018.00597.
- Vennema H, de Groot RJ, Harbour DA, Dalderup M, Gruffydd-Jones T, Horzinek MC. Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization. J Virol. 1990;64(3):1407–09. doi:https://doi.org/10.1128/JVI.64.3.1407-1409.1990.
- Wang SF, Tseng SP, Yen CH, Yang JY, Tsao CH, Shen CW, Chen KH, Liu FT, Liu WT, Chen YM, et al. Antibody-dependent SARS coronavirus infection is mediated by antibodies against spike proteins. Biochem Biophys Res Commun. 2014;451:208–14. doi:https://doi.org/10.1016/j.bbrc.2014.07.090.
- Du L, Tai W, Zhou Y, Jiang S. Vaccines for the prevention against the threat of MERS-CoV. Expert Rev Vaccines. 2016;15(9):1123–34. doi:https://doi.org/10.1586/14760584.2016.1167603.
- Hawkes RA. Enhancement of the infectivity of arboviruses by specific antisera produced in domestic fowls. Aust J Exp Bio Med Sci. 1964;42:465–82. doi:https://doi.org/10.1038/icb.1964.44.
- Quinlan BD, Mou H, Zhang L, Guo Y, He W, Ojha A, Parcells MS, Luo G, Li W, Zhong G, et al. The SARS-CoV-2 receptor-binding domain elicits a potent neutralizing response without antibody-dependent enhancement. bioRxiv Preprint. 2020. doi:https://doi.org/10.1101/2020.04.10.036418.
- DiLillo DJ, Palese P, Wilson PC, Ravetch JV. Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection. J Clin Invest. 2016;126:605–10. doi:https://doi.org/10.1172/JCI84428.
- Yasui F, Kohara M, Kitabatake M, Nishiwaki T, Fujii H, Tateno C, Yoneda M, Morita K, Matsushima K, Koyasu S, et al. Phagocytic cells contribute to the antibody-mediated elimination of pulmonary-infected SARS coronavirus. Virology. 2014;454:157–68. doi:https://doi.org/10.1016/j.virol.2014.02.005.
- Iwasaki A, Yang Y. The potential danger of suboptimal antibody responses in COVID-19. Nat Rev Immunol. 2020. doi:https://doi.org/10.1038/s41577-020-0321-6.
- Takada A, Kawaoka Y. Antibody-dependent enhancement of viral infection: molecular mechanisms and in vivo implications. Rev Med Virol. 2003;13(6):387–98. doi:https://doi.org/10.1002/rmv.405.
- Ruckwardt TJ, Morabito KM, Graham BS. Immunological lessons from respiratory syncytial virus vaccine development. Immunity. 2019;51(3):429–42. doi:https://doi.org/10.1016/j.immuni.2019.08.007.
- Hohdatsu T, Nakamura M, Ishizuka Y, Yamada H, Koyama H. A study on the mechanism of antibody-dependent enhancement of feline infectious peritonitis virus infection in feline macrophages by monoclonal antibodies. Arch Virol. 1991;120(3–4):207–17. doi:https://doi.org/10.1007/BF01310476.
- Takano T, Yamada S, Doki T, Hohdatsu T. Pathogenesis of oral type I feline infectious peritonitis virus (FIPV) infection: antibody-dependent enhancement infection of cats with type I FIPV via the oral route. J Vet Med Sci. 2019;81(6):911–15. doi:https://doi.org/10.1292/jvms.18-0702.
- Taylor A, Foo SS, Bruzzone R, Dinh LV, King NJ, Mahalingam S. Fc receptors in antibody-dependent enhancement of viral infections. Immunol. Rev. 2015;268:340–64. doi:https://doi.org/10.1111/imr.12367.
- Wang Q, Zhang L, Kuwahara K, Li L, Liu Z, Li T, Zhu H, Liu J, Xu Y, Xie J, et al. Immunodominant SARS coronavirus epitopes in humans elicited both enhancing and neutralizing effects on infection in non-human primates. ACS Infect Dis. 2016;2(5):361–76. doi:https://doi.org/10.1021/acsinfecdis.6b00006.
- Tseng CT, Sbrana E, Iwata-Yoshikawa N, Newman PC, Garron T, Atmar RL, Peters CJ, Couch RB. Immunization with SARS coronavirus vaccines leads to pulmonary immunopathology on challenge with the SARS virus. PLoS ONE. 2012;7:e35421. doi:https://doi.org/10.1371/journal.pone.0035421.
- Houser KV, Broadbent AJ, Gretebeck L, Vogel L, Lamirande EW, Sutton T, Bock KW, Minai M, Orandle M, Moore IN, et al. Enhanced inflammation in New Zealand white rabbits when MERS-CoV reinfection occurs in the absence of neutralizing antibody. PLoS Pathog. 2017;13:e1006565. doi:https://doi.org/10.1371/journal.ppat.1006565.
- Smatti MK, Al Thani AA, Yassine HM. Viral-induced enhanced disease illness. Front Microbiol. 2018;9:2991. doi:https://doi.org/10.3389/fmicb.2018.02991.
- Yong CY, Ong HK, Yeap SK, Ho KL, Tan WS. Recent advances in the vaccine development against middle east respiratory syndrome-coronavirus. Front Microbiol. 2019;10:1781. doi:https://doi.org/10.3389/fmicb.2019.01781.
- Padron-Regalado E. Vaccines for SARS-CoV-2: lessons from other coronavirus strains. Infect Dis Ther. 2020. doi:https://doi.org/10.1007/s40121-020-00300-x.
- Wan Y, Shang J, Sun S, Tai W, Chen J, Geng Q, He L, Chen Y, Wu J, Shi Z, et al. Molecular mechanism for antibody-dependent enhancement of coronavirus entry. J Virol. 2020;94:pii: e02015-19.
- Walls AC, Xiong X, Park YJ, Tortorici MA, Snijder J, Quispe J, Cameroni E, Gopal R, Dai M, Lanzavecchia A, et al. Unexpected receptor functional mimicry elucidates activation of coronavirus fusion. Cell. 2019;176(5):1026–1039e15. doi:https://doi.org/10.1016/j.cell.2018.12.028.
- Pierson TC, Fremont DH, Kuhn RJ, Diamond MS. Structural insights into the mechanisms of antibody-mediated neutralization of flavivirus infection: implications for vaccine development. Cell Host Microbe. 2008;4:229–38. doi:https://doi.org/10.1016/j.chom.2008.08.004.
- Tan W, Lu Y, Zhang J, Wang J, Dan Y, Tan Z, He X, Qian X, Sun Q, Hu Q, et al. Viral kinetics and antibody responses in patients with COVID-19. medRxiv. 2020. doi:https://doi.org/10.1101/2020.03.24.20042382.
- Jaume M, Yip MS, Cheung CY, Leung HL, Li PH, Kien F, Dutry I, Callendret B, Escriou N, Altmeyer R, et al. Anti-severe acute respiratory syndrome coronavirus spike antibodies trigger infection of human immune cells via a pH- and cysteine protease-independent FcγR pathway. J. Virol. 2011;85:10582–97. doi:https://doi.org/10.1128/JVI.00671-11.
- Anania JC, Chenoweth AM, Wines BD, Hogarth PM. The human FcγRII (CD32) family of leukocyte FcR in health and disease. Front Immunol. 2019;10:464. doi:https://doi.org/10.3389/fimmu.2019.00464.
- Bharadwaj D, Stein MP, Volzer M, Mold C, Du Clos TW. The major receptor for C-reactive protein on leukocytes is fcgamma receptor II. J Exp Med. 1999;190:585–90. doi:https://doi.org/10.1084/jem.190.4.585.
- Kadkhoda K. COVID-19: an immunopathological view. mSphere. 2020;5(2):pii: e00344-20. doi:https://doi.org/10.1128/mSphere.00344-20.
- Lu R, Zhao X, Li J, Niu P, Yang B, Wu H, Wang W, Song H, Huang B, Zhu N, et al. Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. Lancet. 2020;395(10224):565–74. doi:https://doi.org/10.1016/S0140-6736(20)30251-8.
- Ahmed SF, Quadeer AA, McKay MR. Preliminary identification of potential vaccine targets for the COVID-19 coronavirus (SARS-CoV-2) based on SARS-CoV immunological studies. Viruses. 2020;12(3):pii: E254. doi:https://doi.org/10.3390/v12030254.
- Hua R, Zhou Y, Wang Y, Hua Y, Tong G. Identification of two antigenic epitopes on SARS-CoV spike protein. Biochem Biophys Res Commun. 2004;319:929–35. doi:https://doi.org/10.1016/j.bbrc.2004.05.066.
- Tetro JA. Is COVID-19 receiving ADE from other coronaviruses? Microbes and Infection. 2020;22(2):72–73. doi:https://doi.org/10.1016/j.micinf.2020.02.006.
- Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, Graham BS, McLellan JS. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science. 2020. doi:https://doi.org/10.1126/science.abb2507.
- Tai W, He L, Zhang X, Pu J, Voronin D, Jiang S, Zhou Y, Du L. Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine. Cell Mol Immunol. 2020;17(6):613–20. doi:https://doi.org/10.1038/s41423-020-0400-4.
- Tian X, Li C, Huang A, Xia S, Lu S, Shi Z, Lu L, Jiang S, Yang Z, Wu Y, et al. Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody. Emerg Microbes Infect. 2020;9(1), 382–85. DOI: https://doi.org/10.1080/22221751.2020.1729069.
- Yuan M, Wu NC, Zhu X, Lee CD, So RTY, Lv H, Mok CKP, Wilson IA. A highly conserved cryptic epitope in the receptor-binding domains of SARS-CoV-2 and SARS-CoV. Science. 2020;368(6491):630-33.
- Lv H, Wu NC, Tsang OT, Yuan M, Perera RAPM, Leung WS, So RTY, Chan JMC, Yip GK, Chik TSH Cross-reactive antibody response between SARS-CoV-2 and SARS-CoV infections. Cell Rep. 2020;31(9):107725. doi:https://doi.org/10.1016/j.celrep.2020.107725.
- Elshabrawy HA, Coughlin MM, Baker SC, Prabhakar BS. Human monoclonal antibodies against highly conserved HR1 and HR2 domains of the SARS-CoV spike protein are more broadly neutralizing. PLoS One. 2012;7:e50366. doi:https://doi.org/10.1371/journal.pone.0050366.
- PREVAIL II Writing Group, Multi-National PREVAIL II Study Team,Davey RT Jr, Dodd L, Proschan MA, Neaton J, Neuhaus Nordwall J, Koopmeiners JS, Beigel J, Tierney J, et al. A randomized, controlled trial of ZMapp for ebola virus infection. N Engl J Med. 2016;375:1448–56.
- Du L, Tai W, Yang Y, Zhao G, Zhu Q, Sun S, Liu C, Tao X, Tseng CK, Perlman S, et al. Introduction of neutralizing immunogenicity index to the rational design of MERS coronavirus subunit vaccines. Nat. Commun. 2016;7:13473. doi:https://doi.org/10.1038/ncomms13473.
- Agnihothram S, Gopal R, Yount BL, Donaldson EF, Menachery VD, Graham RL, Scobey TD, Gralinski LE, Denison MR, Zambon M, et al. Evaluation of serologic and antigenic relationships between Middle Eastern respiratory syndrome coronavirus and other coronaviruses to develop vaccine platforms for the rapid response to emerging coronaviruses. J Infect Dis. 2013;209(7):995–1006. doi:https://doi.org/10.1093/infdis/jit609.
- Peeples L. News Feature: avoiding pitfalls in the pursuit of a COVID-19 vaccine. Proc Natl Acad Sci U S A. 2020;117(15):8218–21. doi:https://doi.org/10.1073/pnas.2005456117.
- Li CK, Wu H, Yan H, Ma S, Wang L, Zhang M, Tang X, Temperton NJ, Weiss RA, Brenchley JM, et al. T cell responses to whole SARS coronavirus in humans. J Immunol. 2008;181(8):5490–500. doi:https://doi.org/10.4049/jimmunol.181.8.5490.
- Prompetchara E, Ketloy C, Palaga T. Immune responses in COVID-19 and potential vaccines: lessons learned from SARS and MERS epidemic. Asian Pac J Allergy Immunol. 2020;38(1):1–9. doi:https://doi.org/10.12932/AP-200220-0772.
- de Alwis R, Chen S, Gan ES, Ooi EE. Impact of immune enhancement on Covid-19 polyclonal hyperimmune globulin therapy and vaccine development. EBioMedicine. 2020;55:102768. doi:https://doi.org/10.1016/j.ebiom.2020.102768.
- Hamers-Casterman C, Atarhouch T, Muyldermans S, Robinson G, Hamers C, Songa EB, Bendahman N, Hamers R. Naturally occurring antibodies devoid of light chains. Nature. 1993;363:446–48. doi:https://doi.org/10.1038/363446a0.
- Wilken L, McPherson A. Application of camelid heavy-chain variable domains (VHHs) in prevention and treatment of bacterial and viral infections. Int. Rev. Immunol. 2018;37:69–76. doi:https://doi.org/10.1080/08830185.2017.1397657.
- Chi X, Liu X, Wang C, Zhang X, Ren L, Jin Q, Wang J, Yang W Humanized single domain antibodies neutralize SARS-CoV-2 by targeting spike receptor binding domain. 2020. bioRxiv 2020.04.14.042010; doi: https://doi.org/10.1101/2020.04.14.042010.
- Glab-Ampai K, Chulanetra M, Malik AA, Juntadech T, Thanongsaksrikul J, Srimanote P, Thueng-In K, Sookrung N, Tongtawe P, Chaicumpa W. Human single chain-transbodies that bound to domain-I of non-structural protein 5A (NS5A) of hepatitis C virus. Sci Rep. 2017;7(1):15042. doi:https://doi.org/10.1038/s41598-017-14886-9.
- Eroshenko N, Gill T, Keaveney MK, Church GM, Trevejo JM, Rajaniemi H. Implications of antibody-dependent enhancement of infection for SARS-CoV-2 countermeasures. Nat Biotechnol. 2020 [published online ahead of print, Jun 5];38(7):789–91. doi:https://doi.org/10.1038/s41587-020-0577-1.