Molecular characterization of interactions between the D614G variant of SARS-CoV-2 S-protein and neutralizing antibodies: A computational approach

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dc.contributor.authorKwarteng, Alexander
dc.contributor.authorAsiedu, Ebenezer
dc.contributor.authorSylverken, Augustina Angelina
dc.contributor.authorLarbi, Amma
dc.contributor.authorSakyi, Samuel Asamoah
dc.contributor.authorAsiedu, Samuel Opoku
dc.contributor.orcid0000-0002-0893-2908
dc.contributor.orcid0000-0003-2867-1984
dc.contributor.orcid0000-0002-7691-914X
dc.contributor.orcid0000-0002-3814-6924
dc.contributor.orcid0000-0001-5168-4762
dc.contributor.orcid0000-0002-0352-3195
dc.date.accessioned2024-04-18T10:44:06Z
dc.date.available2024-04-18T10:44:06Z
dc.date.issued2021
dc.descriptionThis is an article published in Infection, Genetics and Evolution 91 (2021) 104815; https://doi.org/10.1016/j.meegid.2021.104815
dc.description.abstractThe D614G variant of SARS-CoV-2 S-protein emerged in early 2020 and quickly became the dominant circulating strain in Europe and its environs. The variant was characterized by the higher viral load, which is not associated with disease severity, higher incorporation into the virion, and high cell entry via ACE-2 and TMPRSS2. Previous strains of the coronavirus and the current SARS-CoV-2 have demonstrated the selection of mutations as a mechanism of escaping immune responses. In this study, we used molecular dynamics simulation and MM-PBSA binding energy analysis to provide insights into the behaviour of the D614G S-protein at the molecular level and describe the neutralization mechanism of this variant. Our results show that the D614G S-protein adopts distinct conformational dynamics which is skewed towards the open-state conformation more than the closed-state conformation of the wild-type S-protein. Residue-specific variation of amino acid flexibility and domain specific RMSD suggest that the mutation causes an allosteric conformational change in the RBD. Evaluation of the interaction energies between the S-protein and neutralizing antibodies show that the mutation may enhance, reduce or not affect the neutralizing interactions depending on the neutralizing antibody, especially if it targets the RBD. The results of this study have shed insights into the behaviour of the D614G S-protein at the molecular level and provided a glimpse of the neutralization mechanism of this variant.
dc.description.sponsorshipKNUST
dc.identifier.citationInfection, Genetics and Evolution 91 (2021) 104815; https://doi.org/10.1016/j.meegid.2021.104815
dc.identifier.urihttps://doi.org/10.1016/j.meegid.2021.104815
dc.identifier.urihttps://ir.knust.edu.gh/handle/123456789/15692
dc.language.isoen
dc.publisherInfection, Genetics and Evolution
dc.titleMolecular characterization of interactions between the D614G variant of SARS-CoV-2 S-protein and neutralizing antibodies: A computational approach
dc.typeArticle
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