Wang Z, Schmidt F, Weisblum Y, Muecksch F, Barnes CO, Finkin S, et al. mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants. Nature. 2021; 592(7855):616-22. [DOI:10.1038/s41586-021-03324-6] [PMID]
Yao Z, Zhang L, Duan Y, Tang X, Lu J. Molecular insights into the adaptive evolution of SARS-CoV-2 spike protein. J Infect. 2024; 88(3):106121. [DOI:10.1016/j.jinf.2024.106121] [PMID]
Coutard B, Valle C, De Lamballerie X, Canard B, Seidah NG, Decroly E. 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. [DOI:10.1016/j.antiviral.2020.104742][PMID]
Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, 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(4):343-55. [DOI:10.1038/s41422-020-0305-x][PMID]
Zhang NN, Zhang RR, Zhang YF, Ji K, Xiong XC, Qin QS, et al. Rapid development of an updated mRNA vaccine against the SARS-CoV-2 Omicron variant. Cell Res. 2022; 32(4):401-3. [DOI:10.1038/s41422-022-00626-w][PMID]
Chen RE, Zhang X, Case JB, Winkler ES, Liu Y, VanBlargan LA, et al. Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies. Nat Med. 2021; 27(4):717-26. [DOI:10.1038/s41591-021-01294-w][PMID]
Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science. 2020; 367(6483):1260-3. [DOI:10.1126/science.abb2507] [PMID]
No Author. DTU Health Tech. ProP 1.0 Server [Internet]. 2026 [Updated 23 Feb 2026]. Available from: [Link]
Yan R, Zhang Y, Li Y, Xia L, Guo Y, Zhou Q. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science. 2020; 367(6485):1444-8. [DOI:10.1126/science.abb2762] [PMID]
Cai Y, Zhang J, Xiao T, Peng H, Sterling SM, Walsh Jr RM, et al. Distinct conformational states of SARS-CoV-2 spike protein. Science. 2020; 369(6511):1586-92. [DOI:10.1126/science.abd4251] [PMID]
Graham RL, Donaldson EF, Baric RS. A decade after SARS: strategies for controlling emerging coronaviruses. Nat Rev Microbiol. 2013; 11(12):836-48. [DOI:10.1038/nrmicro3143][PMID]
Gui M, Song W, Zhou H, Xu J, Chen S, Xiang Y, et al. Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding. Cell Res. 2017; 27(1):119-29. [DOI:10.1038/cr.2016.152] [PMID]
Hoffmann M, Kleine-Weber H, Schroeder S, Krüger N, Herrler T, Erichsen S, et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. cell. 2020; 181(2):271-80. e8. [DOI:10.1016/j.cell.2020.02.052][PMID]
Huang Y, Yang C, Xu XF, Xu W, Liu SW. Structural and functional properties of SARS-CoV-2 spike protein: Potential antivirus drug development for COVID-19. Acta Pharmacol Sin. 2020; 41(9):1141-9. [DOI:10.1038/s41401-020-0485-4][PMID]
Noh JY, Jeong HW, Shin EC. SARS-CoV-2 mutations, vaccines, and immunity: Implication of variants of concern. Signal Transduct Target Ther. 2021; 6(1):203. [DOI:10.1038/s41392-021-00623-2][PMID]
Shang J, Ye G, Shi K, Wan Y, Luo C, Aihara H, et al. Structural basis of receptor recognition by SARS-CoV-2. Nature. 2020; 581(7807):221-4. [DOI:10.1038/s41586-020-2179-y][PMID]
Suryadevara N, Shrihari S, Gilchuk P, VanBlargan LA, Binshtein E, Zost SJ, et al. Neutralizing and protective human monoclonal antibodies recognizing the N-terminal domain of the SARS-CoV-2 spike protein. Cell. 2021; 184(9):2316-31. e15. [DOI:10.1016/j.cell.2021.03.029][PMID]
Thorne LG, Bouhaddou M, Reuschl AK, Zuliani-Alvarez L, Polacco B, Pelin A, et al. Evolution of enhanced innate immune evasion by SARS-CoV-2. Nature. 2022; 602(7897):487-95. [DOI:10.1038/s41586-021-04352-y][PMID]
Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell. 2020; 181(2):281-92. e6. [DOI:10.1016/j.cell.2020.02.058][PMID]
Wang L, Zhou T, Zhang Y, Yang ES, Schramm CA, Shi W, et al. Ultrapotent antibodies against diverse and highly transmissible SARS-CoV-2 variants. Science. 2021; 373(6556):eabh1766. [PMID]
Wang P, Nair MS, Liu L, Iketani S, Luo Y, Guo Y, et al. Antibody resistance of SARS-CoV-2 variants B. 1.351 and B. 1.1. 7. Nature. 2021; 593(7857):130-5. [DOI:10.1038/s41586-021-03398-2][PMID]
Wrobel AG, Benton DJ, Xu P, Roustan C, Martin SR, Rosenthal PB, et al. SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects. Nat Struct Mol Biol. 2020; 27(8):763-7. [DOI:10.1038/s41594-020-0468-7][PMID]
GenBank. Bethesda (MD): National Library of Medicine (US), National Center for Biotechnology Information [Internet]. 1982. Available from: [Link]
GISAID. Global initiative on sharing all influenza data [Internet]. 2026 [Updated 23 Feb 2026] Available from: [Link]
No Author. Molecular evolutionary genetics analysis [Internet]. 2026 [Updated 2026 Feb 23] Available from: [Link]
National Center for Biotechnology Information. NCBI’s 3D Structure Viewer [Internet]. 2026 [Updated 2026 Feb 23] Available from: [Link]
National Center for Biotechnology Information. Molecular Modeling Database [Internet]. 2026 [Updated 2026 Feb 23] Available from: [Link]
Zhang Q, Xiang R, Huo S, Zhou Y, Jiang S, Wang Q, et al. Molecular mechanism of interaction between SARS-CoV-2 and host cells and interventional therapy. Signal Transduct Target Ther. 2021; 6(1):233. [DOI:10.1038/s41392-021-00653-w][PMID]
Cameroni E, Bowen JE, Rosen LE, Saliba C, Zepeda SK, Culap K, et al. Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift. Nature. 2022; 602(7898):664-70. [DOI:10.1038/s41586-021-04386-2][PMID]
Cele S, Gazy I, Jackson L, Hwa SH, Tegally H, Lustig G, et al. Escape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma. Nature. 2021; 593(7857):142-6. [DOI:10.1038/s41586-021-03471-w] [PMID]