Two sides of the same coin: the N-terminal and the receptor binding domains of SARS-CoV-2 Spike
- PMID: 36896145
- PMCID: PMC9987531
- DOI: 10.2217/fvl-2022-0181
Two sides of the same coin: the N-terminal and the receptor binding domains of SARS-CoV-2 Spike
Abstract
The SARS-CoV-2 Spike receptor binding domain and N-terminal domain interact with each other in an intricate mechanism. Mutations modulate the interplay between the Spike and host molecules. This editorial comments on the intricacies of SARS-CoV-2 Spike interactions.
Keywords: AXL; IntAct; N-terminal domain; SARS-CoV-2; Spike; allosteric interaction; electrostatic potential; indels; receptor binding domain; sialoside.
© 2023 Future Medicine Ltd.
Conflict of interest statement
Financial & competing interests disclosure S Pascarella is supported in part by the Sapienza Università di Roma grant (RP12117A7670A1E8). The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed No writing assistance was utilized in the production of this manuscript.The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed
References
-
- Walls AC, Park Y-J, Tortorici MA, Wall A, McGuire AT, Veesler D. Structure, function, and antigenicity of the SARS-CoV-2 Spike glycoprotein. Cell 181(2), 281–292.e6 (2020). - PMC - PubMed
-
•• One of the earliest reports on the characterization of the structure and function of the SARS-CoV-2 Spike protein, and on the comparison with the SARS-CoV spike protein.
-
- Li F. Structure, function, and evolution of coronavirus Spike proteins. Annu. Rev. Virol. 3, 237–261 (2016). - PMC - PubMed
-
• Reviews the structure and function of SARS-CoV spike proteins and discusses the evolution of the critical and specific functions of these proteins, in other words, receptor recognition and membrane fusion.
-
- Harvey WT, Carabelli AM, Jackson B et al. SARS-CoV-2 variants, Spike mutations and immune escape. Nat. Rev. Microbiol. 19(7), 409–424 (2021). - PMC - PubMed
-
•• Review on mutations of the SARS-CoV-2 Spike protein, the primary antigen and their impacts on antigenicity. Discussion is in the context of observed mutation frequencies in global sequence datasets.
-
- Ishikawa T, Ozono H, Akisawa K, Hatada R, Okuwaki K, Mochizuki Y. Interaction analysis on the SARS-CoV-2 Spike protein receptor binding domain using visualization of the interfacial electrostatic complementarity. J. Phys. Chem. Lett. 12(46), 11267–11272 (2021). - PubMed
-
• Quantitative theoretical analysis of the interaction of SARS-COV-2 with angiotensin-converting enzyme (ACE2) and B38 antibody.
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