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Title | Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization. |
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Journal, issue, pages | Cell Host Microbe, Vol. 29, Issue 5, Page 747-751.e4, Year 2021 |
Publish date | May 12, 2021 |
Authors | Pengfei Wang / Ryan G Casner / Manoj S Nair / Maple Wang / Jian Yu / Gabriele Cerutti / Lihong Liu / Peter D Kwong / Yaoxing Huang / Lawrence Shapiro / David D Ho / |
PubMed Abstract | The emergence of SARS-CoV-2 variants has raised concerns about altered sensitivity to antibody-mediated immunity. The relative resistance of SARS-CoV-2 variants B.1.1.7 and B.1.351 to antibody ...The emergence of SARS-CoV-2 variants has raised concerns about altered sensitivity to antibody-mediated immunity. The relative resistance of SARS-CoV-2 variants B.1.1.7 and B.1.351 to antibody neutralization has been recently investigated. We report that another emergent variant from Brazil, P.1, is not only refractory to multiple neutralizing monoclonal antibodies but also more resistant to neutralization by convalescent plasma and vaccinee sera. The magnitude of resistance is greater for monoclonal antibodies than vaccinee sera and evident with both pseudovirus and authentic P.1 virus. The cryoelectron microscopy structure of a soluble prefusion-stabilized spike reveals that the P.1 trimer adopts exclusively a conformation in which one of the receptor-binding domains is in the "up" position, which is known to facilitate binding to entry receptor ACE2. The functional impact of P.1 mutations thus appears to arise from local changes instead of global conformational alterations. The P.1 variant threatens current antibody therapies but less so protective vaccine efficacy. |
External links | Cell Host Microbe / PubMed:33887205 / PubMed Central |
Methods | EM (single particle) |
Structure data | EMDB-23718, PDB-7m8k: |
Chemicals | ChemComp-NAG: |
Source |
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Keywords | VIRAL PROTEIN / Spike Glycoprotein |