Abstract
Virus and host innate immune system interaction plays a significant role in forming the outcome of viral diseases. Host innate immunity initially recognizes the viral invasion and induces a rapid inflammatory response, and this recognition activates signaling cascades that trigger the release of antiviral mediators. This chapter aims to explore the mechanisms by which newly emerged coronavirus called severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) activates the host immune system. Since SARS-CoV-2 shares similarities with SARS-CoV that caused the epidemic of SARS in 2003, the pathogenesis of both viruses could be at least very similar. For this, this chapter provides a synthesis of literature concerning antiviral immunity in SARS-CoV and SARS-CoV-2. It includes the presentation of epitopes linked to SARS-CoV-2 as well as the ability of SARS-CoV-2 to cause proteolytic activation and interact with angiotensin-converting enzyme 2 (ACE2) via molecular mimicry. This chapter characterizes various mechanisms that this virus may engage in escaping the host immunity, ended by a discussion of humoral immune responses against SARS-CoV-2.
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References
Abbas AK, Lichtman AH, Shiv P (2017) Cellular and molecular immunology. Elsevier, Philadelphia
Ahmed S, Quadeer AA, McKay M (2020) Preliminary identification of potential vaccine targets for the COVID-19 coronavirus (SARS-CoV-2) based on SARS-CoV immunological studies. Viruses 12:254. https://doi.org/10.3390/v12030254
Akira S, Uematsu S, Takeuchi O (2006) Pathogen recognition and innate immunity. Cell 124:783–801. https://doi.org/10.1016/j.cell.2006.02.015
Anand P, Puranik A, Aravamudan M et al (2020) SARS-CoV-2 selectively mimics a cleavable peptide of human ENaC in a strategic hijack of host proteolytic. Machinery 2:4–8. https://doi.org/10.1101/2020.04.29.069476
Bailey-Elkin BA, Knaap RCM, Johnson GG et al (2014) Crystal structure of the Middle East respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression. J Biol Chem 289:34667–34682. https://doi.org/10.1074/jbc.M114.609644
Baruah V, Bose S (2020) Immunoinformatics-aided identification of T cell and B cell epitopes in the surface glycoprotein of 2019-nCoV. J Med Virol 92:495–500. https://doi.org/10.1002/jmv.25698
Ben Addi A, Lefort A, Hua X et al (2008) Modulation of murine dendritic cell function by adenine nucleotides and adenosine: involvement of the A(2B) receptor. Eur J Immunol 38:1610–1620. https://doi.org/10.1002/eji.200737781
Berry JD, Jones S, Drebot MA et al (2004) Development and characterisation of neutralising monoclonal antibody to the SARS-coronavirus. J Virol Methods 120:87–96. https://doi.org/10.1016/j.jviromet.2004.04.009
Boucher A, Desforges M, Duquette P, Talbot PJ (2007) Long-term human coronavirus-myelin cross-reactive T-cell clones derived from multiple sclerosis patients. Clin Immunol 123:258–267. https://doi.org/10.1016/j.clim.2007.02.002
Braun J, Loyal L, Frentsch M et al (2020) Presence of SARS-CoV-2 reactive T cells in COVID-19 patients and healthy donors. In: medRxiv 2020.04.17.20061440. https://doi.org/10.1101/2020.04.17.20061440
Cao X (2020) COVID-19: immunopathology and its implications for therapy. Nat Rev Immunol 20:269–270. https://doi.org/10.1038/s41577-020-0308-3
Cappello F (2020) Is COVID-19 a proteiform disease inducing also molecular mimicry phenomena? Cell Stress Chaperones 25(3):381–382. https://doi.org/10.1007/s12192-020-01112-1
Cervantes-Barragan L, Züst R, Weber F et al (2007) Control of coronavirus infection through plasmacytoid dendritic-cell-derived type I interferon. Blood 109(3):1131–1137. https://doi.org/10.1182/blood-2006-05-023770
Cervantes-Barragan L, Lewis KL, Firner S et al (2012) Plasmacytoid dendritic cells control T-cell response to chronic viral infection. Proc Natl Acad Sci 109:3012–3017. https://doi.org/10.1073/pnas.1117359109
Channappanavar R, Fehr AR, Vijay R et al (2016) Dysregulated type I interferon and inflammatory monocyte-macrophage responses cause lethal pneumonia in SARS-CoV-infected mice. Cell Host Microbe 19:181–193. https://doi.org/10.1016/j.chom.2016.01.007
Chen X, Yang X, Zheng Y et al (2014) SARS coronavirus papain-like protease inhibits the type I interferon signaling pathway through interaction with the STING-TRAF3-TBK1 complex. Protein Cell 5:369–381. https://doi.org/10.1007/s13238-014-0026-3
Chen C-F, Chien C-H, Yang Y-P et al (2020) Role of dipeptidyl peptidase 4 inhibitors in diabetic patients with coronavirus-19 infection. J Chin Med Assoc. https://doi.org/10.1097/JCMA.0000000000000338. Publish Ahead of Print
Chew FT, Ong SY, Hew CL (2003) Severe acute respiratory syndrome coronavirus and viral mimicry. Lancet 361:2081. https://doi.org/10.1016/S0140-6736(03)13652-5
Coutard B, Valle C, de Lamballerie X et al (2020) The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade. Antivir Res 176:104742. https://doi.org/10.1016/j.antiviral.2020.104742
Cron RQ, Chatham WW (2020) The rheumatologist’s role in Covid-19. J Rheumatol 200334:639. https://doi.org/10.3899/jrheum.200334
de Wit E, van Doremalen N, Falzarano D, Munster VJ (2016) SARS and MERS: recent insights into emerging coronaviruses. Nat Rev Microbiol 14:523–534. https://doi.org/10.1038/nrmicro.2016.81
Dong C, Ni L, Ye F et al (2020) Characterization of anti-viral immunity in recovered individuals infected by SARS-CoV-2. In: medRxiv 2020.03.17.20036640. https://doi.org/10.1101/2020.03.17.20036640
Dosch SF, Mahajan SD, Collins AR (2009) SARS coronavirus spike protein-induced innate immune response occurs via activation of the NF-kappaB pathway in human monocyte macrophages in vitro. Virus Res 142:19–27. https://doi.org/10.1016/j.virusres.2009.01.005
Ellis N, Li Y, Hildebrand W et al (2005) T cell mimicry and epitope specificity of cross-reactive T cell clones from rheumatic heart disease. J Immunol 175:5448–5456. https://doi.org/10.4049/jimmunol.175.8.5448
Ermolaeva MA, Michallet MC, Papadopoulou N et al (2008) Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIF-dependent inflammatory responses. Nat Immunol 9:1037–1046. https://doi.org/10.1038/ni.1638
Fast E, Altman RB, Chen B (2020) Potential T-cell and B-cell epitopes of 2019-nCoV. In: bioRxiv 2020.02.19.955484. https://doi.org/10.1101/2020.02.19.955484
Felsenstein S, Herbert JA, McNamara PS, Hedrich CM (2020) COVID-19: immunology and treatment options. Clin Immunol 215:108448. https://doi.org/10.1016/j.clim.2020.108448
Frieman M, Yount B, Heise M et al (2007) Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane. J Virol 81:9812–9824. https://doi.org/10.1128/JVI.01012-07
Garcia-Sastre A, Biron CA (2006) Type 1 interferons and the virus-host relationship: a lesson in detente. Science 312(5775):879–882. https://doi.org/10.1126/science.1125676
Grifoni A, Sidney J, Zhang Y et al (2020) A sequence homology and bioinformatic approach can predict candidate targets for immune responses to SARS-CoV-2. Cell Host Microbe 27:671–680. https://doi.org/10.1016/j.chom.2020.03.002
Guo L, Ren L, Yang S et al (2020) Profiling early humoral response to diagnose novel coronavirus disease (COVID-19). Clin Infect Dis 71:778. https://doi.org/10.1093/cid/ciaa310
Hacker H, Karin M (2006) Regulation and function of IKK and IKK-related kinases. Sci STKE 2006:re13. https://doi.org/10.1126/stke.3572006re13
Hacker H, Redecke V, Blagoev B et al (2006) Specificity in toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6. Nature 439:204–207. https://doi.org/10.1038/nature04369
Hamming I, Timens W, Bulthuis MLC et al (2004) Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis. J Pathol 203:631–637. https://doi.org/10.1002/path.1570
Hansen TH, Bouvier M (2009) MHC class I antigen presentation : learning from viral evasion strategies. Nat Rev Immunol 9:503–513. https://doi.org/10.1038/nri2575
He Y, Zhou Y, Wu H et al (2004) Identification of Immunodominant sites on the spike protein of severe acute respiratory syndrome (SARS) coronavirus: implication for developing SARS diagnostics and vaccines. J Immunol 173:4050–4057. https://doi.org/10.4049/jimmunol.173.6.4050
Hoffmann M, Kleine-Weber H, Pöhlmann S (2020a) A multibasic cleavage site in the spike protein of SARS-CoV-2 is essential for infection of human lung cells. Mol Cell 78:779–784.e5. https://doi.org/10.1016/j.molcel.2020.04.022
Hoffmann M, Kleine-Weber H, Schroeder S et al (2020b) SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell 181:271–280.e8. https://doi.org/10.1016/j.cell.2020.02.052
Hung J-T, Yu AL (2019) Chapter 4 - GD2-targeted immunotherapy of Neuroblastoma. In: Ray SKBT-N (ed) Neuroblastoma. Academic Press, pp 63–78. https://doi.org/10.1016/B978-0-12-812005-7.00004-7
Hwa KY, Lin WM, Hou YI, Yeh TM (2007) Molecular mimicry between SARS coronavirus spike protein and human protein. Proc Front Converg Biosci Inf Technol FBIT 2007:294–298. https://doi.org/10.1109/FBIT.2007.108
Jiang S, Hillyer C, Du L (2020) Neutralizing antibodies against SARS-CoV-2 and other human coronaviruses. Trends Immunol 41:545. https://doi.org/10.1016/j.it.2020.04.008
Karikó K, Buckstein M, Ni H, Weissman D (2005) Suppression of RNA recognition by toll-like receptors: the impact of nucleoside modification and the evolutionary origin of RNA. Immunity 23:165–175. https://doi.org/10.1016/j.immuni.2005.06.008
Katze MG, He Y, Gale M Jr (2002) Viruses and interferon: a fight for supremacy. Nat Rev Immunol 2:675–687. https://doi.org/10.1038/nri888
Kawai T, Akira S (2010) The role of pattern-recognition receptors in innate immunity: update on toll-like receptors. Nat Immunol 11:373–384. https://doi.org/10.1038/ni.1863
Kawai T, Takahashi K, Sato S et al (2005) IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. Nat Immunol 6:981–988. https://doi.org/10.1038/ni1243
Kim SY, Jin W, Sood A et al (2020a) Glycosaminoglycan binding motif at S1/S2 proteolytic cleavage site on spike glycoprotein may facilitate novel coronavirus (SARS-CoV-2) host cell entry. In: bioRxiv 2020.04.14.041459. https://doi.org/10.1101/2020.04.14.041459
Kim D, Lee J-Y, Yang J-S et al (2020b) The architecture of SARS-CoV-2 transcriptome. Cell 181:914–921.e10. https://doi.org/10.1016/j.cell.2020.04.011
Kindler E, Thiel V, Weber F (2016) Interaction of SARS and MERS coronaviruses with the anti-viral interferon response. In: Advances in virus research. Elsevier, pp 219–243. https://doi.org/10.1016/bs.aivir.2016.08.006
Kiyotani K, Toyoshima Y, Nemoto K, Nakamura Y (2020) Bioinformatic prediction of potential T cell epitopes for SARS-CoV-2. J Hum Genet 65:569. https://doi.org/10.1038/s10038-020-0771-5
Knoops K, Kikkert M, van den Worm SHE et al (2008) SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum. PLoS Biol 6(9):e226. https://doi.org/10.1371/journal.pbio.0060226
Kopecky-Bromberg SA, MartĂnez-Sobrido L, Frieman M et al (2007) Severe acute respiratory syndrome coronavirus open reading frame (ORF) 3b, ORF 6, and nucleocapsid proteins function as interferon antagonists. J Virol 81(2):548–557. https://doi.org/10.1128/JVI.01782-06
Kumar H, Kawai T, Akira S (2011) Pathogen recognition by the innate immune system. Int Rev Immunol 30:16–34. https://doi.org/10.3109/08830185.2010.529976
Kuri T, Eriksson KK, Putics A et al (2011) The ADP-ribose-1 ″-monophosphatase domains of severe acute respiratory syndrome coronavirus and human coronavirus 229E mediate resistance to anti-viral interferon responses. J Gen Virol 92:1899–1905. https://doi.org/10.1099/vir.0.031856-0
Lazear HM, Schoggins JW, Diamond MS (2019) Shared and distinct functions of type I and type III Interferons. Immunity 50:907–923. https://doi.org/10.1016/j.immuni.2019.03.025
Lessler J, Reich NG, Brookmeyer R et al (2009) Incubation periods of acute respiratory viral infections: a systematic review. Lancet Infect Dis 9:291–300. https://doi.org/10.1016/S1473-3099(09)70069-6
Li G-W, Xie XS (2011) Central dogma at the single-molecule level in living cells. Nature 475:308–315. https://doi.org/10.1038/nature10315
Li W, Moore MJ, Vasilieva N et al (2003) Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 426:450–454. https://doi.org/10.1038/nature02145
Li F, Li W, Farzan M, Harrison SC (2005) Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science 309:1864–1868. https://doi.org/10.1126/science.1116480
Li G, Fan Y, Lai Y et al (2020a) Coronavirus infections and immune responses. J Med Virol 92:424–432. https://doi.org/10.1002/jmv.25685
Li X, Geng M, Peng Y et al (2020b) Molecular immune pathogenesis and diagnosis of COVID-19. J Pharm Anal 10:102–108. https://doi.org/10.1016/j.jpha.2020.03.001
Liu J, Wu P, Gao F et al (2010) Novel Immunodominant peptide presentation strategy : a featured HLA-A * 2402-restricted cytotoxic T-lymphocyte epitope stabilized by Intrachain hydrogen bonds from severe acute respiratory syndrome coronavirus nucleocapsid protein. J Virol 84:11849–11857. https://doi.org/10.1128/JVI.01464-10
Lokugamage KG, Narayanan K, Nakagawa K et al (2015) Middle East respiratory syndrome coronavirus nsp1 inhibits host gene expression by selectively targeting mRNAs transcribed in the nucleus while sparing mRNAs of cytoplasmic origin. J Virol 89:10970–10981. https://doi.org/10.1128/JVI.01352-15
Lokugamage KG, Hage A, Schindewolf C et al (2020) SARS-CoV-2 sensitive to type I interferon pretreatment. BioRxiv. https://doi.org/10.1101/2020.03.07.982264
Long Q-X, Liu B-Z, Deng H-J et al (2020) Antibody responses to SARS-CoV-2 in patients with COVID-19. Nat Med 26:845. https://doi.org/10.1038/s41591-020-0897-1
Lu X, Pan J, Tao J, Guo D (2011) SARS-CoV nucleocapsid protein antagonizes IFN-β response by targeting initial step of IFN-β induction pathway, and its C-terminal region is critical for the antagonism. Virus Genes 42(1):37–45. https://doi.org/10.1007/s11262-010-0544-x
Lu G, Hu Y, Wang Q et al (2013) Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26. Nature 500:227–231. https://doi.org/10.1038/nature12328
Lu R, Zhao X, Li J et al (2020) Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. Lancet 395:565–574. https://doi.org/10.1016/S0140-6736(20)30251-8
Lucchese G (2020) Epitopes for a 2019-nCoV vaccine. Cell Mol Immunol 17:539–540. https://doi.org/10.1038/s41423-020-0377-z
Lucchese G, Flöel A (2020) Molecular mimicry between SARS-CoV-2 and respiratory pacemaker neurons. Autoimmun Rev 102556:102556. https://doi.org/10.1016/j.autrev.2020.102556
Lyons-Weiler J (2020) Pathogenic priming likely contributes to serious and critical illness and mortality in COVID-19 via autoimmunity. J Transl Autoimmun 3:100051. https://doi.org/10.1016/j.jtauto.2020.100051
Maoz-Segal R, Andrade P (2015) Chapter 3 - molecular mimicry and autoimmunity. In: Shoenfeld Y, Agmon-Levin N, Rose AA (eds) Infection and autoimmunity, 2nd edn. Academic Press, Amsterdam, pp 27–44. https://doi.org/10.1016/B978-0-444-63269-2.00054-4
Martin MU, Wesche H (2002) Summary and comparison of the signaling mechanisms of the toll/interleukin-1 receptor family. Biochim Biophys Acta (BBA) - Molecular Cell Res 1592:265–280. https://doi.org/10.1016/S0167-4889(02)00320-8
Matthews KL, Coleman CM, van der Meer Y et al (2014) The ORF4b-encoded accessory proteins of Middle East respiratory syndrome coronavirus and two related bat coronaviruses localize to the nucleus and inhibit innate immune signalling. J Gen Virol 95:874. https://doi.org/10.1099/vir.0.062059-0
Mazaleuskaya L, Veltrop R, Ikpeze N et al (2012) Protective role of toll-like receptor 3-induced type I interferon in murine coronavirus infection of macrophages. Viruses 4:901–923. https://doi.org/10.3390/v4050901
Menachery VD, Eisfeld AJ, Schafer A et al (2014) Pathogenic influenza viruses and coronaviruses utilize similar and contrasting approaches to control interferon-stimulated gene responses. MBio 5:e01174–e01114. https://doi.org/10.1128/mBio.01174-14
Menachery VD, Schäfer A, Burnum-johnson KE et al (2018) MERS-CoV and H5N1 influenza virus antagonize antigen presentation by altering the epigenetic landscape. Proc Natl Acad Sci 115:E1012–E1021. https://doi.org/10.1073/pnas.1706928115
Meylan E, Curran J, Hofmann K et al (2005) Cardif is an adaptor protein in the RIG-I anti-viral pathway and is targeted by hepatitis C virus. Nature 437:1167–1172. https://doi.org/10.1038/nature04193
Mielech AM, Kilianski A, Baez-Santos YM et al (2014) MERS-CoV papain-like protease has deISGylating and deubiquitinating activities. Virology 450:64–70. https://doi.org/10.1016/j.virol.2013.11.040
Ng MHL, Lau K-M, Li L et al (2004) Association of human-leukocyte-antigen class I (B*0703) and class II (DRB1*0301) genotypes with susceptibility and resistance to the development of severe acute respiratory syndrome. J Infect Dis 190:515–518. https://doi.org/10.1086/421523
Nguyen A, David JK, Maden SK et al (2020) Human leukocyte antigen susceptibility map for SARS-CoV-2. J Virol 94. https://doi.org/10.1128/JVI.00510-20
Ni L, Ye F, Cheng M-L et al (2020) Antibody responses to SARS-CoV-2 in patients with COVID-19. Immunity 52:971–977.e3. https://doi.org/10.1016/j.immuni.2020.04.023
Prabakaran P, Gan J, Feng Y et al (2006) Structure of severe acute respiratory syndrome coronavirus receptor-binding domain Complexed with neutralizing antibody. J Biol Chem 281:15829–15836. https://doi.org/10.1074/jbc.M600697200
Prompetchara E, Ketloy C, Palaga T (2020) Immune responses in COVID-19 and potential vaccines: lessons learned from SARS and MERS epidemic. Asian Pacific J Allergy Immunol 38:1–9. https://doi.org/10.12932/ap-200220-0772
Qin C, Zhou L, Hu Z et al (2020) Dysregulation of immune response in patients with coronavirus 2019 (COVID-19) in Wuhan. China Clin Infect Dis 71:762. https://doi.org/10.1093/cid/ciaa248
Qiu T, Mao T, Wang Y et al (2020) Identification of potential cross-protective epitope between a new type of coronavirus (2019-nCoV) and severe acute respiratory syndrome virus. J Genet Genomics 47:115–117. https://doi.org/10.1016/j.jgg.2020.01.003
Rajaiah R, Moudgil KD (2009) Heat-shock proteins can promote as well as regulate autoimmunity. Autoimmun Rev 8:388–393. https://doi.org/10.1016/j.autrev.2008.12.004
Robbiani DF, Gaebler C, Muecksch F et al (2020) Convergent antibody responses to SARS-CoV-2 infection in convalescent individuals. In: bioRxiv 2020.05.13.092619. https://doi.org/10.1101/2020.05.13.092619
Rosenblum MD, Remedios KA, Abbas AK (2015) Mechanisms of human autoimmunity. J Clin Invest 125:2228–2233. https://doi.org/10.1172/JCI78088
Saghazadeh A, Rezaei N (2017) Implications of toll-like receptors in Ebola infection. Expert Opin Ther Targets 4:415–425. https://doi.org/10.1080/14728222.2017.1299128
Shang J, Ye G, Shi K et al (2020) Structural basis of receptor recognition by SARS-CoV-2. Nature 581:221–224. https://doi.org/10.1038/s41586-020-2179-y
Sheahan T, Morrison TE, Funkhouser W et al (2008) MyD88 is required for protection from lethal infection with a mouse-adapted SARS-CoV. PLoS Pathog 4:e1000240. https://doi.org/10.1371/journal.ppat.1000240
Shi C-S, Qi H-Y, Boularan C et al (2014) SARS-coronavirus open reading frame-9b suppresses innate immunity by targeting mitochondria and the MAVS/TRAF3/TRAF6 signalosome. J Immunol 193(6):3080–3089. https://doi.org/10.4049/jimmunol.1303196
Shi Y, Wang Y, Shao C et al (2020) COVID-19 infection: the perspectives on immune responses. Cell Death Differ 27:1451–1454. https://doi.org/10.1038/s41418-020-0530-3
Shivarov V, Petrov PK, Pashov AD (2020) Potential SARS-CoV-2 preimmune IgM epitopes. Front Immunol 11:932. https://doi.org/10.3389/fimmu.2020.00932
Siu K-L, Kok K-H, M-HJ N et al (2009) Severe acute respiratory syndrome coronavirus M protein inhibits type I interferon production by impeding the formation of TRAF3· TANK· TBK1/IKKϵ complex. J Biol Chem 284(24):16202–16209. https://doi.org/10.1074/jbc.M109.008227
Siu K-L, Yeung ML, Kok K-H et al (2014) Middle east respiratory syndrome coronavirus 4a protein is a double-stranded RNA-binding protein that suppresses PACT-induced activation of RIG-I and MDA5 in the innate anti-viral response. J Virol 88(9):4866–4876. https://doi.org/10.1128/JVI.03649-13
Strollo R, Pozzilli P (2020) DPP4 inhibition: preventing SARS-CoV-2 infection and/or progression of COVID-19? Diabetes Metab Res Rev 36. https://doi.org/10.1002/dmrr.3330
Sui J, Li W, Murakami A et al (2004) Potent neutralization of severe acute respiratory syndrome (SARS) coronavirus by a human mAb to S1 protein that blocks receptor association. Proc Natl Acad Sci 101:2536–2541. https://doi.org/10.1073/pnas.0307140101
Sun L, Xing Y, Chen X et al (2012) Coronavirus papain-like proteases negatively regulate anti-viral innate immune response through disruption of STING-mediated signaling. PLoS One 7(2):e30802. https://doi.org/10.1371/journal.pone.0030802
Takaoka A, Wang Z, Choi MK et al (2007) DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response. Nature 448:501–505. https://doi.org/10.1038/nature06013
Takeuchi O, Akira S (2007) Signaling pathways activated by microorganisms. Curr Opin Cell Biol 19:185–191. https://doi.org/10.1016/j.ceb.2007.02.006
Tang F, Quan Y, Xin Z-T et al (2011) Lack of peripheral memory B cell responses in recovered patients with severe acute respiratory syndrome: a six-year follow-up study. J Immunol 186:7264 LP–7267268. https://doi.org/10.4049/jimmunol.0903490
Tay MZ, Poh CM, Rénia L et al (2020) The trinity of COVID-19: immunity, inflammation and intervention. Nat Rev Immunol 20:363–374. https://doi.org/10.1038/s41577-020-0311-8
ter Meulen J, van den Brink EN, Poon LLM et al (2006) Human monoclonal antibody combination against SARS coronavirus: synergy and coverage of escape mutants. PLoS Med 3:e237. https://doi.org/10.1371/journal.pmed.0030237
Tian X, Li C, Huang A et al (2020) Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody. Emerg Microbes Infect 9:382–385. https://doi.org/10.1080/22221751.2020.1729069
Tilocca B, Soggiu A, Sanguinetti M et al (2020) Comparative computational analysis of SARS-CoV-2 nucleocapsid protein epitopes in taxonomically related coronaviruses. Microbes Infect 22:188. https://doi.org/10.1016/j.micinf.2020.04.002
Totura AL, Whitmore A, Agnihothram S et al (2015) Toll-like receptor 3 signaling via TRIF contributes to a protective innate immune response to severe acute respiratory syndrome coronavirus infection. MBio 6:e00638–e00615. https://doi.org/10.1128/mBio.00638-15
Tseng HK, Trejaut JA, Lee H et al (2003) Association of HLA class I with severe acute respiratory syndrome coronavirus infection. BMC Med Genet 4:9. https://doi.org/10.1186/1471-2350-4-9
Vabret N, Britton GJ, Gruber C et al (2020) Immunology of COVID-19: current state of the science. Immunity 52:910. https://doi.org/10.1016/j.immuni.2020.05.002
van den Brink EN, Ter Meulen J, Cox F et al (2005) Molecular and biological characterization of human monoclonal antibodies binding to the spike and nucleocapsid proteins of severe acute respiratory syndrome coronavirus. J Virol 79:1635–1644. https://doi.org/10.1128/JVI.79.3.1635-1644.2005
Van Hemert MJ, van den Worm SHE, Knoops K et al (2008) SARS-coronavirus replication/transcription complexes are membrane-protected and need a host factor for activity in vitro. PLoS Pathog 4(5):e1000054. https://doi.org/10.1371/journal.ppat.1000054
Vanderlugt CL, Miller SD (2002) Epitope spreading in immune-mediated diseases: implications for immunotherapy. Nat Rev Immunol 2:85–95. https://doi.org/10.1038/nri724
Walls AC, Park Y-J, Tortorici MA et al (2020) Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell 181:281–292.e6. https://doi.org/10.1016/j.cell.2020.02.058
Wang Y, Liu L (2016) The membrane protein of severe acute respiratory syndrome coronavirus functions as a novel cytosolic pathogen-associated molecular pattern to promote Beta interferon induction via a toll-like-receptor-related TRAF3-independent mechanism. MBio 7:e01872–e01815. https://doi.org/10.1128/mBio.01872-15
Wang S-F, Chen K-H, Chen M et al (2011) Human-leukocyte antigen class I Cw 1502 and class II DR 0301 genotypes are associated with resistance to severe acute respiratory syndrome (SARS) infection. Viral Immunol 24:421–426. https://doi.org/10.1089/vim.2011.0024
Wang Q, Qiu Y, Li J-Y et al (2020) A unique protease cleavage site predicted in the spike protein of the novel pneumonia coronavirus (2019-nCoV) potentially related to viral transmissibility. Virol Sin 35:337. https://doi.org/10.1007/s12250-020-00212-7
Weiskopf D, Schmitz KS, Raadsen MP et al (2020) Phenotype of SARS-CoV-2-specific T-cells in COVID-19 patients with acute respiratory distress syndrome. In: medRxiv 2020.04.11.20062349, vol 5. https://doi.org/10.1101/2020.04.11.20062349
Wheatland R (2004) Molecular mimicry of ACTH in SARS - implications for corticosteroid treatment and prophylaxis. Med Hypotheses 63:855–862. https://doi.org/10.1016/j.mehy.2004.04.009
Wu A, Peng Y, Huang B et al (2020) Genome composition and divergence of the novel coronavirus (2019-nCoV) originating in China. Cell Host Microbe 27:325–328. https://doi.org/10.1016/j.chom.2020.02.001
Xu LG, Wang YY, Han KJ et al (2005) VISA is an adapter protein required for virus-triggered IFN-beta signaling. Mol Cell 19:727–740. https://doi.org/10.1016/j.molcel.2005.08.014
Yang J, James E, Roti M et al (2009) Searching immunodominant epitopes prior to epidemic: HLA class II-restricted SARS-CoV spike protein epitopes in unexposed individuals. Int Immunol 21:63–71. https://doi.org/10.1093/intimm/dxn124
Yang Y, Zhang L, Geng H et al (2013) The structural and accessory proteins M, ORF 4a, ORF 4b, and ORF 5 of Middle East respiratory syndrome coronavirus (MERS-CoV) are potent interferon antagonists. Protein Cell 4:951–961. https://doi.org/10.1007/s13238-013-3096-8
Yang Y, Ye F, Zhu N et al (2015) Middle East respiratory syndrome coronavirus ORF4b protein inhibits type I interferon production through both cytoplasmic and nuclear targets. Sci Rep 5:17554. https://doi.org/10.1038/srep17554
Yi Y, Lagniton PNP, Ye S et al (2020) COVID-19: what has been learned and to be learned about the novel coronavirus disease. Int J Biol Sci 16(10):1753–1766. https://doi.org/10.7150/ijbs.45134
Yuan M, Wu NC, Zhu X et al (2020) A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV. Science 368(6491):630–633. https://doi.org/10.1126/science.abb7269
Zeng F, Dai C, Cai P et al (2020) A comparison study of SARS-CoV-2 IgG antibody between male and female COVID-19 patients: a possible reason underlying different outcome between gender. J Med Virol 92:2050. https://doi.org/10.1002/jmv.25989
Zhang B, Zhou X, Zhu C et al (2020) Immune phenotyping based on neutrophil-to-lymphocyte ratio and IgG predicts disease severity and outcome for patients with COVID-19. In: medRxiv 2020.03.12.20035048. https://doi.org/10.1101/2020.03.12.20035048
Zheng M, Song L (2020) Novel antibody epitopes dominate the antigenicity of spike glycoprotein in SARS-CoV-2 compared to SARS-CoV. Cell Mol Immunol 17:536–538. https://doi.org/10.1038/s41423-020-0385-z
Zheng M, Gao Y, Wang G et al (2020) Functional exhaustion of anti-viral lymphocytes in COVID-19 patients. Cell Mol Immunol 17:533–535. https://doi.org/10.1038/s41423-020-0402-2
Zhou H, Chen X, Hu T et al (2020a) A novel bat coronavirus closely related to SARS-CoV-2 contains natural insertions at the S1/S2 cleavage site of the spike protein. Curr Biol 30:2196–2203.e3. https://doi.org/10.1016/j.cub.2020.05.023
Zhou P, Yang X-L, Wang X-G et al (2020b) A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature 579:270–273. https://doi.org/10.1038/s41586-020-2012-7
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Akbarpour, M., Sharifi, L., Safdarian, A.R., Farhangnia, P., Borjkhani, M., Rezaei, N. (2021). Potential Antiviral Immune Response Against COVID-19: Lessons Learned from SARS-CoV. In: Rezaei, N. (eds) Coronavirus Disease - COVID-19. Advances in Experimental Medicine and Biology, vol 1318. Springer, Cham. https://doi.org/10.1007/978-3-030-63761-3_9
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