Differences and similarities between SARS-CoV and SARS-CoV-2: spike receptor-binding domain recognition and host cell infection with support of cellular serine proteases.
Angiotensin-Converting Enzyme 2
Antibodies, Viral
/ biosynthesis
Betacoronavirus
/ immunology
COVID-19
Cathepsins
/ genetics
Coronavirus Infections
/ enzymology
Enzyme Activation
/ immunology
Humans
Immune Evasion
Pandemics
Peptidyl-Dipeptidase A
/ genetics
Pneumonia, Viral
/ enzymology
Protein Binding
Protein Domains
Severe acute respiratory syndrome-related coronavirus
/ immunology
SARS-CoV-2
Serine Endopeptidases
/ genetics
Severe Acute Respiratory Syndrome
/ enzymology
Severity of Illness Index
Spike Glycoprotein, Coronavirus
/ chemistry
Virus Internalization
Virus Replication
Coronavirus
Furin
Receptor binding domain
Sars-CoV
Sars-CoV-2
Journal
Infection
ISSN: 1439-0973
Titre abrégé: Infection
Pays: Germany
ID NLM: 0365307
Informations de publication
Date de publication:
Oct 2020
Oct 2020
Historique:
received:
15
06
2020
accepted:
19
07
2020
pubmed:
2
8
2020
medline:
8
10
2020
entrez:
2
8
2020
Statut:
ppublish
Résumé
Novel severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) became pandemic by the end of March 2020. In contrast to the 2002-2003 SARS-CoV outbreak, which had a higher pathogenicity and lead to higher mortality rates, SARSCoV-2 infection appears to be much more contagious. Moreover, many SARS-CoV-2 infected patients are reported to develop low-titer neutralizing antibody and usually suffer prolonged illness, suggesting a more effective SARS-CoV-2 immune surveillance evasion than SARS-CoV. This paper summarizes the current state of art about the differences and similarities between the pathogenesis of the two coronaviruses, focusing on receptor binding domain, host cell entry and protease activation. Such differences may provide insight into possible intervention strategies to fight the pandemic.
Identifiants
pubmed: 32737833
doi: 10.1007/s15010-020-01486-5
pii: 10.1007/s15010-020-01486-5
pmc: PMC7393809
doi:
Substances chimiques
Antibodies, Viral
0
Spike Glycoprotein, Coronavirus
0
Cathepsins
EC 3.4.-
Peptidyl-Dipeptidase A
EC 3.4.15.1
ACE2 protein, human
EC 3.4.17.23
Angiotensin-Converting Enzyme 2
EC 3.4.17.23
Serine Endopeptidases
EC 3.4.21.-
TMPRSS2 protein, human
EC 3.4.21.-
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
665-669Références
Li Q, Guan X, Wu P, et al. Early transmission dynamics in Wuhan, China, of novel coronavirus-infected pneumonia. N Engl J Med. 2020;382:1199–207.
pubmed: 31995857
pmcid: 31995857
doi: 10.1056/NEJMoa2001316
Yang Y, Peng F, Wang R, et al. The deadly coronaviruses: the 2003 SARS pandemic and the 2020 novel coronavirus epidemic in China. J Autoimmun. 2020;109:102434.
pubmed: 32143990
pmcid: 7126544
doi: 10.1016/j.jaut.2020.102434
Zhou F, Yu T, Du R, et al. Clinical course and risk factors for mortality of adult inpatients with COVID-19 in Wuhan, China: a retrospective cohort study. Lancet. 2020;395:1054–62.
pubmed: 32171076
pmcid: 7270627
doi: 10.1016/S0140-6736(20)30566-3
Shang J, Wan Y, Luo C, et al. Cell entry mechanisms of SARS-CoV-2. Proc Natl Acad Sci USA. 2020;117:11727–34. https://doi.org/10.1073/pnas.2003138117
pubmed: 32376634
doi: 10.1073/pnas.2003138117
Neuman BW, Adair BD, Yoshioka C, Quispe JD, Orca G, Kuhn P, et al. Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy. J Virol. 2006;80:7918–28.
pubmed: 16873249
pmcid: 1563832
doi: 10.1128/JVI.00645-06
Goldsmith CS, Tatti KM, Ksiazek TG, et al. Ultrastructural characterization of SARS coronavirus. Emerg Infect Dis. 2004;10:320–6.
pubmed: 15030705
pmcid: 3322934
doi: 10.3201/eid1002.030913
Fehr AR, Perlman S. Coronaviruses: an overview of their replication and pathogenesis. In: Maier HJ, Bickerton E, Britton P, editors. Coronaviruses. Methods in molecular biology, vol 1282. Berlin: Springer; 2015. p. 1–23.
Heald-Sargent T, Gallagher T. Ready, set, fuse! The coronavirus spike protein and acquisition of fusion competence. Viruses. 2012;4:557–80.
pubmed: 22590686
pmcid: 3347323
doi: 10.3390/v4040557
Follis KE, York J, Nunberg JH. Furin cleavage of the SARS coronavirus spike glycoprotein enhances cell-cell fusion but does not affect virion entry. Virology. 2006;350:358–69.
pubmed: 16519916
pmcid: 7111780
doi: 10.1016/j.virol.2006.02.003
Simmons G, Zmora P, Gierer S, et al. Proteolytic activation of the SARS-coronavirus spike protein: cutting enzymes at the cutting edge of antiviral research. Antiviral Res. 2013;100:605–14.
pubmed: 24121034
pmcid: 3889862
doi: 10.1016/j.antiviral.2013.09.028
Lai MM, Cavanagh D. The molecular biology of coronaviruses. Adv Virus Res. 1997;48:1–100.
pubmed: 9233431
pmcid: 7130985
doi: 10.1016/S0065-3527(08)60286-9
Astuti I, Ysrafil Y. severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2): an overview of viral structure and host response. Diabetes Metab Syndr. 2020;14:407–12.
pubmed: 32335367
pmcid: 7165108
doi: 10.1016/j.dsx.2020.04.020
Neuman BW, Buchmeier MJ. Supramolecular architecture of the coronavirus particle. Adv Virus Res. 2016;96:1–27.
pubmed: 27712621
pmcid: 7112365
doi: 10.1016/bs.aivir.2016.08.005
Chen Y, Liu Q, Guo D. Emerging coronaviruses: genome structure, replication, and pathogenesis. J Med Virol. 2020;92:418–23.
pubmed: 31967327
pmcid: 7167049
doi: 10.1002/jmv.25681
Tortorici MA, Veesler D. Structural insights into coronavirus entry. Adv Virus Res. 2019;105:93–116.
pubmed: 31522710
pmcid: 7112261
doi: 10.1016/bs.aivir.2019.08.002
Wang LF, Shi Z, Zhang S, Field H, et al. Review of bats and SARS. Emerg Infect Dis. 2006;12:1834–40.
pubmed: 17326933
pmcid: 3291347
doi: 10.3201/eid1212.060401
Xu J, Zhao S, Teng T, et al. Systematic comparison of two animal-to-human transmitted human coronaviruses: SARS-CoV-2 and SARS-CoV. Viruses. 2020;12:244.
pmcid: 7077191
doi: 10.3390/v12020244
Li W, Moore MJ, Vasilieva N, et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature. 2003;426:450–4.
pubmed: 14647384
pmcid: 7095016
doi: 10.1038/nature02145
Yan R, Zhang Y, Li Y, Xia L, et al. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science. 2020;367:1444–8.
pubmed: 32132184
pmcid: 7164635
doi: 10.1126/science.abb2762
Shang J, Ye G, Shi K, et al. Structural basis of receptor recognition by SARS-CoV-2. Nature. 2020;581:221–4.
pubmed: 32225175
doi: 10.1038/s41586-020-2179-y
Yuan Y, Cao D, Zhang Y, et al. Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains. Nat Commun. 2017;8:15092.
pubmed: 28393837
pmcid: 5394239
doi: 10.1038/ncomms15092
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;5:562–9.
pubmed: 32094589
doi: 10.1038/s41564-020-0688-y
Ou X, Liu Y, Lei X, et al. Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV. Nat Commun. 2020;11:1620.
pubmed: 32221306
pmcid: 7100515
doi: 10.1038/s41467-020-15562-9
Gui M, Song W, Zhou H, et al. Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding. Cell Res. 2017;27:119–29.
pubmed: 28008928
doi: 10.1038/cr.2016.152
Xia S, Liu M, Wang C, et al. Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. Cell Res. 2020;30:343–55.
pubmed: 32231345
doi: 10.1038/s41422-020-0305-x
Gheblawi M, Wang K, Viveiros A, et al. Angiotensin-converting enzyme 2: SARS-CoV-2 receptor and regulator of the renin-angiotensin system: celebrating the 20th anniversary of the discovery of ACE2. Circ Res. 2020;126:1456–74.
pubmed: 32264791
doi: 10.1161/CIRCRESAHA.120.317015
Ortiz-Fernandez L, Sawalha AH. Genetic variability in the expression of SARS-CoV-2 host cell entry factors across populations. bioRxiv. 2020. https://doi.org/10.1101/2020.04.06.027698 .
doi: 10.1101/2020.04.06.027698
Belouzard S, Millet JK, Licitra BN, et al. Mechanisms of coronavirus cell entry mediated by the viral spike protein. Viruses. 2012;4:1011–33.
pubmed: 22816037
pmcid: 3397359
doi: 10.3390/v4061011
Rabaan AA, Al-Ahmed SH, Haque S, et al. SARS-CoV-2, SARS-CoV, and MERS-COV: a comparative overview. Infez Med. 2020;28:174–84.
pubmed: 32275259
Hasöksüz M, Kiliç S, Saraç F. Coronaviruses and SARS-COV-2. Turk J Med Sci. 2020;50:549–56.
pubmed: 32293832
pmcid: 7195990
doi: 10.3906/sag-2004-127
Liu J, Zheng X, Tong Q, et al. Overlapping and discrete aspects of the pathology and pathogenesis of the emerging human pathogenic coronaviruses SARS-CoV, MERS-CoV, and 2019-nCoV. J Med Virol. 2020;92:491–4.
pubmed: 32056249
pmcid: 7166760
doi: 10.1002/jmv.25709
Hoffmann M, Kleine-Weber H, et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell. 2020;181:271–80.
pubmed: 32142651
pmcid: 32142651
doi: 10.1016/j.cell.2020.02.052
Coutard B, Valle C, de Lamballerie X, et al. The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade. Antiviral Res. 2020;176:104742.
pubmed: 32057769
pmcid: 7114094
doi: 10.1016/j.antiviral.2020.104742
Hoffmann M, Kleine-Weber H, Pöhlmann S. A multibasic cleavage site in the spike protein of SARS-CoV-2 is essential for infection of human lung cells. Mol Cell. 2020;78(4):779–784.e5. https://doi.org/10.1016/j.molcel.2020.04.022 .
pubmed: 32362314
pmcid: 7194065
doi: 10.1016/j.molcel.2020.04.022
Li F, Berardi M, Li W, et al. Conformational states of the severe acute respiratory syndrome coronavirus spike protein ectodomain. J Virol. 2006;80:6794–800.
pubmed: 16809285
pmcid: 1489032
doi: 10.1128/JVI.02744-05
Walls AC, Park YJ, Tortorici MA, et al. Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell. 2020;181:281–92.
pubmed: 32155444
pmcid: 7102599
doi: 10.1016/j.cell.2020.02.058
Liu C, Yang Y, Gao Y, et al. Viral architecture of SARS-CoV-2 with post-fusion spike revealed by Cryo-EM. bioRxiv. https://doi.org/10.1101/2020.03.02.972927 .
Millet JK, Whittaker GR. Host cell proteases: citical determinants of coronavirus tropism and pathogenesis. Virus Res. 2015;202:120–34.
pubmed: 25445340
doi: 10.1016/j.virusres.2014.11.021
Kawase M, Shirato K, van der Hoek L, Taguchi F, Matsuyama S. Simultaneous treatment of human bronchial epithelial cells with serine and cysteine protease inhibitors prevents severe acute respiratory syndrome coronavirus entry. J Virol. 2012;86:6537–45.
pubmed: 22496216
pmcid: 3393535
doi: 10.1128/JVI.00094-12
McKee DL, Sternberg A, Stange U, Laufer S, Naujokat C. Candidate drugs against SARS-CoV-2 and COVID-19. Pharmacol Res. 2020;157:104859.
pubmed: 32360480
pmcid: 7189851
doi: 10.1016/j.phrs.2020.104859
McFadyen JD, Stevens H, Peter K. The emerging threat of (micro)thrombosis in COVID-19 and its therapeutic implications. Circ Res. 2020;10:1161 (published online ahead of print, 2020 Jun 26).