Molecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants.
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) transmission leads to the emergence of variants, including the B.1.617.2 (Delta) variant of concern that is causing a new wave of infections and has become globally dominant. We show that these variants dampen the in vitro potency of vaccine-elicited serum neutralizing antibodies and ... provide a structural framework for describing their immune evasion. Mutations in the B.1.617.1 (Kappa) and Delta spike glycoproteins abrogate recognition by several monoclonal antibodies via alteration of key antigenic sites, including remodeling of the Delta amino-terminal domain. The angiotensin-converting enzyme 2 binding affinities of the Kappa and Delta receptor binding domains are comparable to the Wuhan-Hu-1 isolate, whereas B.1.617.2+ (Delta+) exhibits markedly reduced affinity.
Mesh Terms:
2019-nCoV Vaccine mRNA-1273, Ad26COVS1, Angiotensin-Converting Enzyme 2, Antibodies, Neutralizing, Antibodies, Viral, Antigens, Viral, BNT162 Vaccine, COVID-19 Vaccines, Cryoelectron Microscopy, Humans, Immune Evasion, Models, Molecular, Mutation, Protein Binding, Protein Conformation, Protein Domains, Protein Folding, Receptors, Coronavirus, SARS-CoV-2, Spike Glycoprotein, Coronavirus
2019-nCoV Vaccine mRNA-1273, Ad26COVS1, Angiotensin-Converting Enzyme 2, Antibodies, Neutralizing, Antibodies, Viral, Antigens, Viral, BNT162 Vaccine, COVID-19 Vaccines, Cryoelectron Microscopy, Humans, Immune Evasion, Models, Molecular, Mutation, Protein Binding, Protein Conformation, Protein Domains, Protein Folding, Receptors, Coronavirus, SARS-CoV-2, Spike Glycoprotein, Coronavirus
Science
Date: Dec. 24, 2021
PubMed ID: 34751595
View in: Pubmed Google Scholar
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