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Structural Evaluation of the Spike Glycoprotein Variants on SARS-CoV-2 Transmission and Immune Evasion
Salleh, Mohd Zulkifli; orcid: 0000-0003-4069-9381; email: m.z.salleh@usm.my Derrick, Jeremy P.; email: jeremy.derrick@manchester.ac.uk Deris, Zakuan Zainy; orcid: 0000-0003-3344-1518; email: zakuan@usm.my
Salleh, Mohd Zulkifli; orcid: 0000-0003-4069-9381; email: m.z.salleh@usm.my
Derrick, Jeremy P.; email: jeremy.derrick@manchester.ac.uk
Deris, Zakuan Zainy; orcid: 0000-0003-3344-1518; email: zakuan@usm.my
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2021-07-10
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Abstract: The emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) presents significant social, economic and political challenges worldwide. SARS-CoV-2 has caused over 3.5 million deaths since late 2019. Mutations in the spike (S) glycoprotein are of particular concern because it harbours the domain which recognises the angiotensin-converting enzyme 2 (ACE2) receptor and is the target for neutralising antibodies. Mutations in the S protein may induce alterations in the surface spike structures, changing the conformational B-cell epitopes and leading to a potential reduction in vaccine efficacy. Here, we summarise how the more important variants of SARS-CoV-2, which include cluster 5, lineages B.1.1.7 (Alpha variant), B.1.351 (Beta), P.1 (B.1.1.28/Gamma), B.1.427/B.1.429 (Epsilon), B.1.526 (Iota) and B.1.617.2 (Delta) confer mutations in their respective spike proteins which enhance viral fitness by improving binding affinity to the ACE2 receptor and lead to an increase in infectivity and transmission. We further discuss how these spike protein mutations provide resistance against immune responses, either acquired naturally or induced by vaccination. This information will be valuable in guiding the development of vaccines and other therapeutics for protection against the ongoing coronavirus disease 2019 (COVID-19) pandemic.
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International Journal of Molecular Sciences, volume 22, issue 14, page e7425
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MDPI
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From MDPI via Jisc Publications Router
History: accepted 2021-07-07, pub-electronic 2021-07-10
Publication status: Published
Funder: Universiti Sains Malaysia; Grant(s): 1001/PPSP/8012382
History: accepted 2021-07-07, pub-electronic 2021-07-10
Publication status: Published
Funder: Universiti Sains Malaysia; Grant(s): 1001/PPSP/8012382