The evil role of spike in the coronaviruses: structure, function and evolution

1. 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 2. Zhou P, Tachedjian M, Wynne JW, et al (2016) Contraction of the type i IFN locus and unusual constitutive expression of IFN-α in bats. Proc Natl Acad Sci U S A 113:2696–2701 . doi: 10.1073/pnas.1518240113 3. 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 . doi: 10.1016/j.chom.2020.02.001 4. Singhal T (2020) A Review of Coronavirus Disease-2019 (COVID-19). 87:281–286 5. Lai MC (2007) Coronaviridae. Fields Virol 1305–1318 6. Adams MJ, King AMQ, Carstens EB (2013) Ratification vote on taxonomic proposals to the International Committee on Taxonomy of Viruses (2013). Arch Virol 158:2023–2030 7. van Regenmortel MH V, Fauquet CM, Bishop DHL, et al (2000) Virus taxonomy: classification and nomenclature of viruses. Seventh report of the International Committee on Taxonomy of Viruses. Academic Press 8. Rockett R (2010) Human coronaviruses. PCR Clin Microbiol An Aust Int Perspect 273–275 . doi: 10.1007/978-90-481-9039-3_42 9. Andersen KG, Rambaut A, Lipkin WI, et al (2020) The proximal origin of SARS-CoV-2. Nat Med 2–4 . doi: 10.1038/s41591-020-0820-9 10. Wang L, Wang Y, Ye D, Liu Q (2020) A review of the 2019 Novel Coronavirus (COVID-19) based on current evidence. Int J Antimicrob Agents 105948 . doi: 10.1016/j.ijantimicag.2020.105948 11. Carter J, Saunders V, Saunders VA (2007) Virology: principles and applications. John Wiley & Sons 12. Alsaadi EAJ, Jones IM (2019) Membrane binding proteins of coronaviruses. 14:275–286 13. Li F (2016) Structure, Function, and Evolution of Coronavirus Spike Proteins. Annu Rev Virol 3:237–261 . doi: 10.1146/annurev-virology-110615-042301 14. Hoffmann M, Kleine-Weber H, Schroeder S, et al (2020) SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell 1–10 . doi: 10.1016/j.cell.2020.02.052 15. Masters PS (2006) The molecular biology of coronaviruses. Adv Virus Res 66:193–292 16. Li F (2012) Evidence for a common evolutionary origin of coronavirus spike protein receptor-binding subunits. J Virol 86:2856–2858 17. Peng G, Sun D, Rajashankar KR, et al (2011) Crystal structure of mouse coronavirus receptor-binding domain complexed with its murine receptor. Proc Natl Acad Sci 108:10696–10701 18. Schwegmann-Weßels C, Herrler G (2006) Sialic acids as receptor determinants for coronaviruses. Glycoconj J 23:51–58 19. Chen Y, Rajashankar KR, Yang Y, et al (2013) Crystal Structure of the Receptor-Binding Domain from Newly Emerged Middle East Respiratory Syndrome Coronavirus. J Virol 87:10777–10783 . doi: 10.1128/jvi.01756-13 20. Tortorici MA, Veesler D (2019) Structural insights into coronavirus entry, 1st ed. Elsevier Inc. 21. Millet JK, Whittaker GR (2015) Host cell proteases: Critical determinants of coronavirus tropism and pathogenesis. Virus Res 202:120–134 22. Wrapp D, Wang N, Corbett KS, et al (2020) Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science (80- ) 367:1260–1263 23. Zhou P, Yang X-L, Wang X-G, et al (2020) A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature 579:270–273 24. Ge X-Y, Li J-L, Yang X-L, et al (2013) Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor. Nature 503:535–538 25. Li F, Li W, Farzan M, Harrison SC (2005) Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science (80- ) 309:1864–1868 26. Towler P, Staker B, Prasad SG, et al (2004) ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis. J Biol Chem 279:17996–18007 27. Lu G, Wang Q, Gao GF (2015) Bat-to-human: spike features determining ‘host jump’of coronaviruses SARS-CoV, MERS-CoV, and beyond. Trends Microbiol 23:468–478 28. Hou Y, Peng C, Yu M, et al (2010) Angiotensin-converting enzyme 2 (ACE2) proteins of different bat species confer variable susceptibility to SARS-CoV entry. Arch Virol 155:1563–1569 29. Li W, Greenough TC, Moore MJ, et al (2004) Efficient replication of severe acute respiratory syndrome coronavirus in mouse cells is limited by murine angiotensin-converting enzyme 2. J Virol 78:11429–11433 30. Graham RL, Baric RS (2010) Recombination, reservoirs, and the modular spike: mechanisms of coronavirus cross-species transmission. J Virol 84:3134–3146 31. Qu X-X, Hao P, Song X-J, et al (2005) Identification of two critical amino acid residues of the severe acute respiratory syndrome coronavirus spike protein for its variation in zoonotic tropism transition via a double substitution strategy. J Biol Chem 280:29588–29595 32. Reguera J, Mudgal G, Santiago C, Casasnovas JM (2014) A structural view of coronavirus–receptor interactions. Virus Res 194:3–15 33. Frana MF, Behnke JN, Sturman LS, Holmes K V (1985) Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: host-dependent differences in proteolytic cleavage and cell fusion. J Virol 56:912–920 34. Shulla A, Heald-Sargent T, Subramanya G, et al (2011) A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry. J Virol 85:873–882 35. Park JE, Li K, Barlan A, et al (2016) Proteolytic processing of middle east respiratory syndrome coronavirus spikes expands virus tropism. Proc Natl Acad Sci U S A 113:12262–12267 . doi: 10.1073/pnas.1608147113 36. Li H, Wu C, Yang Y, et al (2020) Furin, a potential therapeutic target for COVID-19. ChinaXiv 202002.00062 . doi: 10.12074/202002.00062 37. Wu C, Yang Y, Liu Y, Zhang P Furin , a potential therapeutic target for COVID-19. doi 10.12074/202002.00062 38. Walls AC, Tortorici MA, Snijder J, et al (2017) Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion. Proc Natl Acad Sci 114:11157–11162 39. Zhang H, Penninger JM, Li Y, et al (2020) Angiotensin-converting enzyme 2 (ACE2) as a SARS-CoV-2 receptor: molecular mechanisms and potential therapeutic target. Intensive Care Med 46:586–590 . doi: 10.1007/s00134-020-05985-9 40. 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 41. 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 0036-8075. doi  10.1126/science.abb7269     The evil role of spike in the coronaviruses: structure, function and evolution Ghavamipour F.1, Nasrollahi P. 1, Dabirmanesh B.1, Jalili H.2 and Khajeh Kh.1 1 Dept. of Biochemistry, Tarbiat Modares University, Tehran, I.R. of Iran 2 Dept. of Life Science Engineering, University of Tehran, Tehran, I.R. of Iran Abstract Since the beginning of the 21st century, coronaviruses that originated from animals to human have been the cause of several deadly pneumonia epidemics including SARS, MERS disease, and now COVID-19 which has become a worldwide pandemic. The emergence of these acute respiratory syndromes emphasizes the cross-species transmission of coronaviruses and their prevalence in humans. Coronaviruses contain a surface- spike protein (S) that initiates infection by recognizing its receptor and attaching to the membrane, which is a key step in the host specificity and intergenerational transmission. To date, no specific treatment or vaccine against any of the seven human coronaviruses has been approved. This underscores the importance of exploring the mechanisms governing the virus entry and intergenerational transmission. This review article discuss the mechanism of infection used by coronaviruses by focusing on the features of the S protein and its receptor binding characteristics in different species. In addition, protease processes involved in the onset of infection was considered to provide a complete picture of their role in the coronavirus replication cycle. Finally, treatments based on the interaction of S-protein and ACE2 receptor were described.