Mutations in S2 subunit of SARS-CoV-2 Omicron spike strongly influence its conformation, fusogenicity, and neutralization sensitivity.
Omicron
SARS-CoV-2
neutralizing antibodies
spike conformation
spike protein
virus entry
Journal
Journal of virology
ISSN: 1098-5514
Titre abrégé: J Virol
Pays: United States
ID NLM: 0113724
Informations de publication
Date de publication:
30 Nov 2023
30 Nov 2023
Historique:
medline:
1
12
2023
pubmed:
20
10
2023
entrez:
20
10
2023
Statut:
ppublish
Résumé
The Omicron subvariants have substantially evaded host-neutralizing antibodies and adopted an endosomal route of entry. The virus has acquired several mutations in the receptor binding domain and N-terminal domain of S1 subunit, but remarkably, also incorporated mutations in S2 which are fixed in Omicron sub-lineage. Here, we found that the mutations in the S2 subunit affect the structural and biological properties such as neutralization escape, entry route, fusogenicity, and protease requirement.
Identifiants
pubmed: 37861334
doi: 10.1128/jvi.00922-23
pmc: PMC10688319
doi:
Substances chimiques
Antibodies, Neutralizing
0
Antibodies, Viral
0
Endopeptidases
EC 3.4.-
Peptide Hydrolases
EC 3.4.-
Spike Glycoprotein, Coronavirus
0
spike protein, SARS-CoV-2
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0092223Subventions
Organisme : DST | Science and Engineering Research Board (SERB)
ID : IPA/2020/000168
Organisme : Council of Scientific and Industrial Research, India (CSIR)
Organisme : CSIR-Institute of Genomics and Integrative Biology
ID : MLP-2005
Organisme : Fondation Botnar (Botnar Foundation)
ID : CLP-0031
Déclaration de conflit d'intérêts
R.V. and R.S. are inventors on a patent application for RBD and Spike antigens used in this study; other authors declare no conflict of interest.
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