Russian Journal of Infection and ImmunityRussian Journal of Infection and ImmunityИнфекция и иммунитет2220-76192313-7398SPb RAACI144310.15789/2220-7619-CAU-1443REVIEWSОБЗОРЫCOVID-19: an updated reviewCOVID-19: обновленный взглядhttps://orcid.org/0000-0002-6409-3969IsihakF. A.ИсихакФ. А.
Iraq

Assistant Professor, Department of Microbiology, College of Veterinary Medicine

Mosul

доцент кафедры микробиологии Колледжа ветеринарной медицины

г. Мосул

fanar1976@yahoo.comhttps://orcid.org/0000-0001-9278-5391HamadM. A.ХамадМ. А.
Iraq

Mohammad A. Hamad – Assistant Professor, Department of Microbiology, College of Veterinary Medicine

Al Majmoaa Street, MosulPhone: +964 77 28214770 

Мохаммад А. Хамад – доцент кафедры микробиологии Колледжа ветеринарной медицины

г. Мосул, ул. Аль-МаджмоаТел.: +964 77 28214770

mahmah1073@gmail.comhttps://orcid.org/0000-0002-8351-1230MustafaN. G.МустафаН. Г.
Iraq

Professor, Head of Department of Physiology, Biochemistry, and Pharmacology, College of Veterinary Medicine

Mosul

профессор, зав. кафедрой физиологии, биохимии и фармакологии Колледжа ветеринарной медицины

г. Мосул

nashaat_ghalib@yahoo.comUniversity of MosulУниверситет Мосула220520201022472580404202006042020Copyright ©; 2020, Isihak F.A., Hamad M.A., Mustafa N.G.Copyright ©; 2020, Исихак Ф.А., Хамад М.А., Мустафа Н.Г.2020Isihak F.A., Hamad M.A., Mustafa N.G.Исихак Ф.А., Хамад М.А., Мустафа Н.Г.https://creativecommons.org/licenses/by/4.0https://iimmun.ru/iimm/article/view/1443

COVID-19 is a zoonotic disease that showed higher levels of transmissibility in humans. Coronavirus has the largest recognized genome (28–33 kb) of a positive-sense single stranded RNA. The genome composed of 5′-end, the translationable mRNA sequences for the key proteins; replicase, spike, envelop membrane, and nucleocapsid and 3′-end (polyA tail). This highly contagious virus may impair the immune system in the early phase of the disease, hence the symptoms of the disease appear very rapidly. Importantly until now, there is no efficient strategy for containing the disease. So, all the world scientists today are in a race against time to find a vaccine or treatment to COVID-19, which requires a deeper understanding.

COVID-19 является зоонозным заболеванием, для которого обнаружен более высокий уровень передачи у человека. Среди всех РНК-содержащих вирусов коронавирусы имеют наибольший размер генома (28–33 п.о.), представленный положительно-полярной нитью РНК. В частности, их геном содержит 5′-конец, транслируемые мРНК, соответствующие ключевым белкам; репликазу, белок spike (шип), белки оболочки, нуклеокапсид и 3′-конец (поли-A хвост). Этот высококонтагиозный вирус может влиять на иммунную систему на ранней стадии инфекции, из-за чего симптомы заболевания проявляются очень быстро. Важно, что до сих пор отсутствует эффективная стратегия по ограничению этого заболевания. Исходя из этого, ученые всего мира в гонке со временем заняты поиском вакцин или методов лечения COVID-19, что требует более глубокого понимания течения заболевания.

COVID-19SARS-CoV-2vaccinationvirus structureepidemiologyACE2spikesCOVID-19SARS-CoV-2вакцинациястроение вирусаэпидемиологияACE2шипы1. Agier J., Efenberger M., Brzezi ń ska-B ł aszczyk E. Cathelicidin impact on inflammatory cells. Cent. Eur. J. Immunol., 2015, vol. 40, pp. 225–235.2. Ahmed A., Siman-Tov G., Hall G., Bhalla N., Narayanan A. Human antimicrobial peptides as therapeutics for viral infections. Viruses, 2019, vol. 11: 704. doi: 10.3390/v110807043. Almeida J.D., Tyrrell D.A. The morphology of three previously uncharacterized human respiratory viruses that grow in organ culture. J. Gen. Virol., 1967, vol. 1, pp. 175–178.4. Andersen K.G., Rambaut A., Lipkin W.I., Holmes E.C., Garry R.F. The proximal origin of SARS-CoV-2. Nat. Med., 2020. doi: 10.1038/s41591-020-0820-95. André P., Denis C., Soulas C., Bourbon-Caillet C., Lopez J., Arnoux T., Bléry M., Bonnafous C., Gauthier L., Morel A., Rossi B., Remark R., Breso V., Bonnet E., Habif G., Guia S., Lalanne A.I., Hoffmann C., Lantz O., Fayette J., Boyer-Chammard A., Zerbib R., Dodion P., Ghadially H., Jure-Kunkel M., Morel Y., Herbst R., Narni-Mancinelli E., Cohen R.B., Vivier E. Anti-NKG2A mAb is a checkpoint inhibitor that promotes anti-tumor immunity by unleashing both T and NK cells. Cell, 2018, vol. 7, pp. 1731–1743. doi: 10.1016/j.cell.2018.10.0146. Arabi Y., Balkhy H., Hajeer A.H., Bouchama A., Hayden F.G., Al-Omari A., Al-Hameed F.M., Taha Y., Shindo N., Whitehead J., Merson L., AlJohani S., Al-Khairy K., Carson G., Luke T.C., Hensley L., Al-Dawood A., Al-Qahtani S., Modjarrad K., Sadat M., Rohde G., Leport C., Fowler R. Feasibility, safety, clinical, and laboratory effects of convalescent plasma therapy for patients with Middle East respiratory syndrome coronavirus infection: a study protocol. Springerplus, 2015, vol. 4, p. 709. doi: 10.1186/s40064015-1490-97. Báez-Santos Y.M., John S.E.S., Mesecar A.D. The SARS-coronavirus papain-like protease: structure, function and inhibition by designed antiviral compounds. Antiviral Res., 2015, vol. 115, pp. 21–38. doi: 10.1016/j.antiviral.2014.12.0158. Beisswenger C., Bals R. Antimicrobial peptides in lung inflammation. Chem. Immunol. Allergy, 2005, vol. 86, pp. 55–71. doi: 10.1159/0000866519. Bosch B.J., van der Zee R., de Haan C.A., Rottier P.J. The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex. J. Virol., 2003, vol. 77, pp. 8801–8811. doi: 10.1128/jvi.77.16.88018811.200310. Caly L., Druce J.D., Catton M.G., Jans D.A., Wagstaff K.M. The FDA approved drug ivermectin inhibits the replication of SARSCoV-2 in vitro. Antiviral Res., 2020: 104787. doi: 10.1016/j.antiviral.2020.10478711. Casadevall A., Pirofski L. The convalescent sera option for containing COVID-19. J. Clin. Invest., 2020, vol. 130, no. 4, pp. 15451548. doi: 10.1172/JCI13800312. CDC. In the absence of SARS-CoV transmission worldwide: guidance for surveillance, clinical and laboratory evaluation, and reporting version 2. URL: https://www.cdc.gov/sars/surveillance/absence.pdf13. CDC. Interim clinical guidance for management of patients with confirmed coronavirus disease (COVID-19). URL: https://www.cdc.gov/coronavirus/2019-ncov/hcp/clinical-guidance-management-patients.html14. Chan J.F., Kok K.H., Zhu Z., Chu H., To K.K., Yuan S., Yuen K.Y. Genomic characterization of the 2019 novel human-pathogenic coronavirus isolated from a patient with atypical pneumonia after visiting Wuhan. Emerg. Microbes Infect., 2020, vol. 9, pp. 221–236. doi: 10.1080/22221751.2020.171990215. Chan K.H., Chan J.F., Tse H., Chen H., Lau C.C., Cai J.P., Tsang A.K., Xiao X., To K.K., Lau S.K., Woo P.C., Zheng B.J., Wang M., Yuen K.Y. Cross-reactive antibodies in convalescent SARS patients’ sera against the emerging novel human coronavirus EMC (2012) by both immunofluorescent and neutralizing antibody tests. J. Infect., 2013, vol. 67, pp. 130–140.16. Chen N., Zhou M., Dong X., Qu J., Gong F., Han Y., Qiu Y., Wang J., Liu Y., Wei Y., Xia J., Yu T., Zhang X., Zhang L. Epidemiological and clinical characteristics of 99 cases of 2019 novel coronavirus pneumonia in Wuhan, China: a descriptive study. Lancet, 2020, vol. 395, pp. 507–513. doi: 10.1016/S0140-6736(20)30211-717. De la Fuente-Nunez C., Silva O.N., Lu T.K., Franco O.L. Antimicrobial peptides: role in human disease and potential as immunotherapies. Pharmacol. Ther., 2017, vol. 178, pp. 132–140.18. Du L., Zhao G., Kou Z., Ma C., Sun S., Poon V.K., Lu L., Wang L., Debnath A.K., Zheng B.J., Zhou Y., Jiang S. Identification of a receptor-binding domain in the S protein of the novel human coronavirus Middle East respiratory syndrome coronavirus as an essential target for vaccine development. J. Virol., 2013, vol. 87, pp. 9939–9942.19. Durbin R.K., Kotenko S.V., Durbin J.E. Interferon induction and function at the mucosal surface. Immunol. Rev., 2013, vol. 255, pp. 25–39. doi: 10.1111/imr.1210120. FDA. Coronavirus Disease 2019 (COVID-19). URL: https://www.fda.gov/emergency-preparedness-and-response/counterterrorismand-emerging-threats/coronavirus-disease-2019-covid-1921. Fehr A.R., Perlman S. Coronaviruses: an overview of their replication and pathogenesis. Methods Mol. Biol., 2015, vol. 1282, pp. 1–23. doi: 10.1007/978-1-4939-2438-7-122. Fine P., Eames K., Heymann D.L. Herd Immunity: a rough guide. Clin. Infect. Dis., 2011, vol. 52, pp. 911–916. doi: 10.1093/cid/cir00723. Flint J., Racaniello V.R., Rall G.F., Skalka A.M. Principles of virology. 4 th ed. Washington, DC: ASAM Press, 2015.24. Forni D., Cagliani R., Clerici M., Sironi M. Molecular evolution of Human Coronavirus genomes. Trends Microbiol., 2017, vol. 25, pp. 35–48. doi: 10.1016/j.tim.2016.09.00125. Gonzá lez-Garc í a M., St ä ndker L., Otero-Gonz á lez A.J. Antimicrobial peptides in multiresistant respiratory infections. Rev. Cubana Med. Trop., 2019, vol. 71, no. 2, pp. 1–16.26. Gralinski L.E., Menachery V.D. Return of the coronavirus: 2019-nCoV. Viruses, 2020, vol. 12, p. 2. doi: 10.3390/v1202013527. Hofmann H, Simmons G., Rennekamp AJ, Chaipan C., Gramberg T., Heck E., Geier M., Wegele A., Marzi A., Bates P., Pöhlmann S. Highly conserved regions within the spike proteins of human coronaviruses 229E and NL63 determine recognition of their respective cellular receptors. J. Virol., 2006, vol. 80, pp. 8639–8652.28. Hsieh N., Hartshorn K.L. The role of antimicrobial peptides in influenza virus infection and their potential as antiviral and immunomodulatory therapy. Pharmaceuticals (Basel), 2016, vol. 9, pp. 3. doi: 10.3390/ph903005329. Huang C., Wang Y., Li X., Ren L., Zhao J., Hu Y., Zhang L., Fan G., Xu J., Gu X., Cheng Z., Yu T., Xia J., Wei Y., Wu W., Xie X., Yin W., Li H., Liu M., Xiao Y., Gao H., Guo L., Xie J., Wang G., Jiang R., Gao Z., Jin Q., Wang J., Cao B. Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China. Lancet, 2020, vol. 395, pp. 497–506. doi: 10.1016/S01406736(20)30183-530. Jin Y.H., Cai L., Cheng Z.S., Cheng H., Deng T., Fan Y.P., Fang C., Huang D., Huang L.Q., Huang Q., Han Y., Hu B., Hu F., Li B.H., Li Y.R., Liang K., Lin L.K., Luo L.S., Ma J., Ma L.L., Peng Z.Y., Pan Y.B., Pan Z.Y., Ren X.Q., Sun H.M., Wang Y., Wang Y.Y., Weng H., Wei C.J., Wu D.F., Xia J., Xiong Y., Xu H.B., Yao X.M., Yuan Y.F., Ye T.S., Zhang X.C., Zhang Y.W., Zhang Y.G., Zhang H.M., Zhao Y., Zhao M.J., Zi H., Zeng X.T., Wang Y.Y., Wang X.H.; for the Zhongnan Hospital of Wuhan University Novel Coronavirus Management and Research Team, Evidence-Based Medicine Chapter of China International Exchange and Promotive Association for Medical and Health Care (CPAM). A rapid advice guideline for the diagnosis and treatment of 2019 novel coronavirus (2019-nCoV) infected pneumonia (standard version). Mil. Med. Res., 2020, vol. 7, no. 4. doi: 10.1186/s40779-020-0233-631. Kahn J., McIntosh K. History and recent advances in coronavirus discovery. Pediatr. Infect. Dis. J., 2005, vol. 24, iss. 11, pp. S223-S227. doi: 10.1097/01.inf.0000188166.17324.6032. Kikkert M. Innate immune evasion by human respiratory RNA viruses. J. Innate Immun., 2020, vol. 12, pp. 4–20. doi: 10.1159/00050303033. Lai M.M., Holmes K.V. Coronaviridae: the viruses and their replication. In: Fields Virology. Eds. Knipe D.M., Howley P.M. Philadelphia, PA: Lippincott-Raven, 2001.34. Lai M.M., Holmes K.V. Coronaviruses. In: Fields Virology. Eds.: Knipe D.M., Howley P.M., Griffin D.E., Lamb R.A., Martin M.A., Roizman B., Straus S.E. Philadelphia, PA: Lippincott Williams & Wilkins, 2001, pp. 1163–1185.35. Lei J., Kusov Y, Hilgenfeld R. Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein. Antiviral Res., 2018, vol. 149, pp. 58–74.36. 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, vol. 10, pp. 562–569. doi: 10.1038/s41564-020-0688-y37. Lewicki D.N., Gallagher T.M. Quaternary structure of coronavirus spikes in complex with carcino embryonic antigen-related cell adhesion molecule cellular receptors. J. Biol. Chem., 2002, vol. 277, pp. 19727–19734. doi: 10.1074/jbc.M201837200.38. Li F. Structural analysis of major species barriers between humans and palm civets for severe acute respiratory syndrome coronavirus infections. J. Virol., 2008, vol. 82, pp. 6984–6991.39. Li F. Structure, function, and evolution of coronavirus spike proteins. Annu. Rev. Virol., 2016, vol. 3, pp. 237–261. doi: 10.1146/annurev-virology-110615-04230140. Li Q., Guan X., Wu P., Wang X., Zhou L., Tong Y., Ren R., Leung K.S.M., Lau E.H.Y., Wong J.Y., Xing X., Xiang N., Wu Y., Li C., Chen Q., Li D., Liu T., Zhao J., Liu M., Tu W., Chen C., Jin L., Yang R., Wang Q., Zhou S., Wang R., Liu H., Luo Y., Liu Y., Shao G., Li H., Tao Z., Yang Y., Deng Z., Liu B., Ma Z., Zhang Y., Shi G., Lam T.T.Y., Wu J.T., Gao G.F., Cowling B.J., Yang B., Leung G.M., Feng Z. Early transmission dynamics in Wuhan, China, of novel coronavirus-infected pneumonia. N. Engl. J. Med., 2020, vol. 382, pp. 1199–1207. doi: 10.1056/NEJMoa200131641. Li S.W., Wang C.Y., Jou Y.J., Huang S.H., Hsiao L.H., Wan L., Lin Y.J., Kung S.H., Lin C.W. SARS coronavirus papain-like protease inhibits the TLR7 signaling pathway through removing Lys63-linked polyubiquitination of TRAF3 and TRAF6. Int. J. Mol. Sci., 2016, vol. 17, no. 5, p. 678. doi: 10.3390/ijms1705067842. Li W., Hulswit R.J.G., Widjaja I., Raj V.S., McBride R., Peng W., Widagdo W., Tortorici M.A., van Dieren B., Lang Y., van Lent J.W.M., Paulson J.C., de Haan C.A.M., de Groot R.J., van Kuppeveld F.J.M., Haagmans B.L., Bosch B.J. Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein. Proc. Natl. Acad. Sci., 2017, vol. 114, pp. E8508–E8517. doi: 10.1073/pnas.171259211443. Lin H.X., Feng Y., Wong G., Wang L., Li B., Zhao X., Li Y., Smaill F., Zhang C. Identification of residues in the receptor-binding domain (RBD) of the spike protein of human coronavirus NL63 that are critical for the RBD–ACE2 receptor interaction. J. Gen. Virol., 2008, vol. 89, pp. 1015–1024. doi: 10.1099/vir.0.83331-044. Liu C., Tang J., Ma Y., Liang X., Yang Y., Peng G., Qi Q., Jiang S., Li J., Du L., Li F. Receptor usage and cell entry of porcine epidemic diarrhea coronavirus. J. Virol., 2015, vol. 89, pp. 6121–6125.45. Lu H. Drug treatment options for the 2019-new coronavirus (2019-nCoV). Biosci. Trends., 2020, vol. 14, pp. 69–71. doi: 10.5582/bst.2020.0102046. Lu R., Zhao X., Li J., Niu P., Yang B., Wu H., Wang W., Song H., Huang B., Zhu N., Bi Y., Ma X., Zhan F., Wang L., Hu T., Zhou H., Hu Z., Zhou W., Zhao L., Chen J., Meng Y., Wang J., Lin Y., Yuan J., Xie Z., Ma J., Liu W.J., Wang D., Xu W., Holmes E.C., Gao G.F., Wu G., Chen W., Shi W., Tan W. Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. Lancet, 2020, vol. 395, no. 10224, pp. 565–574. doi: 10.1016/S01406736(20)30251-847. Luke T.C., Kilbane E.M., Jackson J.L., Hoffman S.L. Meta-analysis: convalescent blood products for Spanish influenza pneumonia: a future H5N1 treatment? Ann. Intern. Med., 2006, vol. 145, pp. 599–609.48. Mair-Jenkins J., Saavedra-Campos M., Baillie J.K., Cleary P., Khaw F.M., Lim W.S., Makki S., Rooney K.D., Nguyen-VanTam J.S., Beck C.R.; Convalescent Plasma Study Group. The effectiveness of convalescent plasma and hyperimmune immunoglobulin for the treatment of severe acute respiratory infections of viral etiology: a systematic review and exploratory meta-analysis. J. Infect. Dis., 2015, vol. 211, pp. 80–90. doi: 10.1093/infdis/jiu39649. Mou H., Raj V.S., van Kuppeveld F.J., Rottier P.J., Haagmans B.L., Bosch B.J. The receptor binding domain of the new MERS coronavirus maps to a 231-residue region in the spike protein that efficiently elicits neutralizing antibodies. J. Virol., 2013, vol. 87, pp. 9379–9383. doi: 10.1128/JVI.01277-1350. Mupapa K., Massamba M., Kibadi K., Kuvula K., Bwaka A., Kipasa M. Treatment of Ebola hemorrhagic fever with blood transfusions from convalescent patients. International Scientific and Technical Committee. J. Infect. Dis., 1999, vol. 179, pp. 18–23.51. Muramatsu T., Takemoto C., Kim Y.T., Wang H., Nishii W., Terada T., Shirouzu M., Yokoyama S. SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity. Proc. Natl. Acad. Sci. USA, 2016, vol. 113, pp. 1299713002. doi: 10.1073/pnas.160132711352. Newton A.H., Cardani A., Braciale T.J. The host immune response in respiratory virus infection: balancing virus clearance and immunopathology. Semin. Immunopathol., 2016, vol. 38, pp. 471–482. doi: 10.1007/s00281-016-0558-053. Niemeyer D., M ö sbauer K., Klein E.M., Sieberg A., Mettelman R.C., Mielech A.M., Dijkman R., Baker S.C., Drosten C., Müller M.A. The papain-like protease determines a virulence trait that varies among members of the SARS-coronavirus species. PLoS Pathog., 2018, vol. 14: e1007296. doi: 10.1371/journal.ppat.100729654. Nour R., Houssam S. Middle East respiratory syndrome coronavirus (MERS-CoV): a review. Germs, 2019, vol. 9, pp. 35–42. doi: 10.18683/germs.2019.115555. Peng G., Xu L., Lin Y.L., Chen L., Pasquarella J.R., Holmes K.V., Li F. Crystal structure of bovine coronavirus spike protein lectin domain. J. Biol. Chem., 2012, vol. 287, pp. 41931–41938. doi: 10.1074/jbc.M112.41821056. Promkuntod N., van Eijndhoven R.E., de Vrieze G., Gr ö ne A., Verheije M.H. Mapping of the receptor-binding domain and amino acids critical for attachment in the spike protein of avian coronavirus infectious bronchitis virus. Virology, 2014, vol. 448, pp. 26–32.57. Raj V.S., Mou H., Smits S.L., Dekkers D.H., Müller M.A., Dijkman R., Muth D., Demmers J.A., Zaki A., Fouchier R.A., Thiel V., Drosten C., Rottier P.J., Osterhaus A.D., Bosch B.J., Haagmans B.L. Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC. Nature, 2013, vol. 495, pp. 251–254. doi: 10.1038/nature1200558. Reddy K.V., Yedery R.D., Aranha C. Antimicrobial peptides: premises and promises. Int. J. Antimicrob. Agents, 2004, vol. 24, pp. 536–547. doi: 10.1016/j.ijantimicag.2004.09.005PMID1555587459. Rothana H.A., Byrareddy S.N. The epidemiology and pathogenesis of coronavirus disease (COVID-19) outbreak. J. Autoimmun., 2020, vol. 109: 102433. doi: 10.1016/j.jaut.2020.10243360. Sah R., Rodriguez-Morales A.J., Jha R., Chu D.K.W, Gu H., Peiris M., Bastola A., Lal B.K., Ojha H.C., Rabaan A.A., Zambrano L.I., Costello A., Morita K., Pandey B.D., Poon L.L.M. Complete Genome Sequence of a 2019 Novel Coronavirus (SARS-CoV-2) Strain Isolated in Nepal. Microbiol. Resour. Announc., 2020, vol. 9: e00169-20. doi: 10.1128/MRA.00169-2061. Samuel C.E . Antiviral actions of interferons. Clin. Microbiol. Rev., 2001, vol. 14, pp. 778–809. doi: 10.1128/CMR.14.4.778-809.200162. Shanmugaraj B., Siriwattananon K., Wangkanont K., Phoolcharoen W. Perspectives on monoclonal antibody therapy as potential therapeutic intervention for Coronavirus disease-19 (COVID-19). Asian Pac. J. Allergy Immunol., 2020, vol. 38, pp. 10–18. doi: 10.12932/AP-200220-077363. Shi Y., Wang Y., Shao C., Huang J., Gan J., Huang X., Bucci E., Piacentini M., Ippolito G., Melino G. COVID-19 infection: the perspectives on immune responses. Cell Death Differ., 2020. doi: 10.1038/s41418-020-0530-364. Snijder E.J., Decroly E., Ziebuhr J. The nonstructural proteins directing coronavirus RNA synthesis and processing. Adv. Virus Res., 2016, vol. 96, pp. 59–126. doi: 10.1016/bs.aivir.2016.08.00865. Song W., Gui M., Wang X., Xiang Y. Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. PLoS Pathog., 2018, vol. 14, no. 8: e1007236. doi: 10.1371/journal.ppat.100723666. Su S.,Wong G., Shi W., Liu J., Lai A.C.K., Zhou J., Liu W., Bi Y., Gao G.F. Epidemiology, genetic recombination, and pathogenesis of coronaviruses. Trends Microbiol., 2016, vol. 24, pp. 490–502.67. Subissi L., Imbert I., Ferron F., Collet A., Coutard B., Decroly E., Canard B. SARS-CoV ORF1b-encoded nonstructural proteins 12-16: replicative enzymes as antiviral targets. Antiviral Res., 2014, vol. 101, pp. 122–130. doi: 10.1016/j.antiviral.2013.11.00668. Tang X., Wu C., Li X., Song Y., Yao X., Wu X., Duan Y., Zhang H., Wang Y., Qian Z., Cui J., Lu J. On the origin and continuing evolution of SARS-CoV-2. Natl. Sci. Rev., 2020. doi: 10.1093/nsr/nwaa03669. Tyrrell D.A., Bynoe M.L. Cultivation of viruses from a high proportion of patients with colds. Lancet, 1966, vol. 1, pp. 76–77.70. Verschueren K.H., Pumpor K., Anemüller S., Chen S., Mesters J.R., Hilgenfeld R. a structural view of the inactivation of the SARS coronavirus main proteinase by benzotriazole esters. Chem. Biol., 2008, vol. 15, pp. 597–606.71. Walls A.C., Tortorici M.A., Snijder J., Xiong X., Bosch B.J., Rey F.A., Veesler D. Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion. Proc. Natl. Acad. Sci., 2017, vol. 114, pp. 11157–11162. doi: 10.1073/pnas.1708727114.72. Wang L.F., Shi Z., Zhang S., Field H., Daszak P., Eaton B.T. Review of Bats and SARS. Emerg. Infect. Dis., 2006, vol. 12, pp. 12.73. Wang W., Tang J., Wei F. Updated understanding of the outbreak of 2019 novel coronavirus (2019-nCoV) in Wuhan, China. J. Med. Virol., 2020, vol. 92, pp. 441–447. doi: 10.1002/jmv.25689.74. Wilder-Smith A., Teleman M.D., Heng B.H., Earnest A., Ling A.E., Leo Y.S. Asymptomatic SARS coronavirus infection among healthcare workers, Singapore. Emerg. Infect. Dis., 2005, vol. 11, pp. 1142–1145. doi: 10.3201/eid1107.04116575. Wilson M.E., Chen L.H. Travelers give wings to novel coronavirus (2019-nCoV). J. Travel Med., 2020, vol. 27, iss. 2: taaa015. doi: 10.1093/jtm/taaa01576. World Health Organization. Clinical management of severe acute respiratory infection when novel coronavirus (2019-nCoV) infection is suspected: Interim guidance. 28 January 2020. URL: https://apps.who.int/iris/handle/10665/33089377. Wrapp D., Wang N., Corbett K.S., Goldsmith J.A., Hsieh C.L., Abiona O., Graham B.S., McLellan J.S. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science, 2020, vol. 367, pp. 1260–1263. doi: 10.1126/science.abb2507.78. Wu F., Zhao S., Yu B., Chen Y.M., Wang W., Song Z.G., Hu Y., Tao Z.W., Tian J.H., Pei Y.Y., Yuan M.L., Zhang Y.L., Dai F.H., Liu Y., Wang Q.M., Zheng J.J., Xu L., Holmes E.C., Zhang Y.Z. A new coronavirus associated with human respiratory disease in China. Nature, 2020, vol. 579, pp. 265–269. doi: 10.1038/s41586-020-2008-379. Yang Y., Du L., Liu C., Wang L., Ma C., Tang J., Baric R.S., Jiang S., Li F. Receptor usage and cell entry of bat coronavirus HKU4 provide insight into bat-to-human transmission of MERS coronavirus. PNAS, 2014, vol. 111, pp. 12516–12521. doi: 10.1073/pnas.140588911180. Yeh K.M., Chiueh T.S., Siu L.K., Lin J.C., Chan P.K., Peng M.Y., Wan H.L., Chen J.H., Hu B.S., Perng C.L., Lu J.J., Chang F.Y. Experience of using convalescent plasma for severe acute respiratory syndrome among healthcare workers in a Taiwan hospital. J. Antimicrob. Chemother., 2005, vol. 56, pp. 919–922.81. Yount N.Y., André s M.T., Fierro J.F., Yeaman M.R. The gamma-core motif correlates with antimicrobial activity in cysteinecontaining kaliocin-1 originating from transferrins. Biochim. Biophys. Acta, 2007, vol. 1768, pp. 2862–2872.82. Yuan L., Chen Z., Song S., Wang S., Tian C., Xing G., Chen X., Xiao Z.X., He F., Zhang L. p53 degradation by a coronavirus papain-like protease suppresses type I interferon signaling. J. Biol. Chem., 2015, vol. 290, pp. 3172–3182. doi: 10.1074/jbc.M114.61989083. Zhang C., Wang X.M., Li S.R., Twelkmeyer T., Wang W.H., Zhang S.Y., Wang S.F., Chen J.Z., Jin X., Wu Y.Z., Chen X.W., Wang S.D., Niu J.Q., Chen H.R., Tang H. NKG2A is a NK cell exhaustion checkpoint for HCV persistence. Nat. Commun., 2019, vol. 10, no. 1: 1507. doi: 10.1038/s41467-019-09212-y84. Zheng M., Gao Y., Wang G., Song G., Liu S., Sun D., Xu Y., Tian Z. Functional exhaustion of antiviral lymphocytes in COVID-19 patients. Cell. Mol. Immunol., 2020. doi: 10.1038/s41423-020-0402-285. Zhou P., Yang X.L., Wang X.G., Hu B., Zhang L., Zhang W., Si H.R., Zhu Y., Li B., Huang C.L., Chen H.D., Chen J., Luo Y., Guo H., Jiang R.D., Liu M.Q., Chen Y., Shen X.R., Wang X., Zheng X.S., Zhao K., Chen Q.J., Deng F., Liu L.L., Yan B., Zhan F.X., Wang Y.Y., Xiao G.F., Shi Z.L. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature, 2020, vol. 579, no. 7798, pp. 270–273. doi: 10.1038/s41586-020-2012-7