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Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization

Cell host & microbe, 2021-05, Vol.29 (5), p.747-751.e4 [Peer Reviewed Journal]

2021 Elsevier Inc. ;Copyright © 2021 Elsevier Inc. All rights reserved. ;2021 Elsevier Inc. 2021 Elsevier Inc. ;ISSN: 1931-3128 ;EISSN: 1934-6069 ;DOI: 10.1016/j.chom.2021.04.007 ;PMID: 33887205

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Title:
Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization
Author: Wang, Pengfei ; Casner, Ryan G. ; Nair, Manoj S. ; Wang, Maple ; Yu, Jian ; Cerutti, Gabriele ; Liu, Lihong ; Kwong, Peter D. ; Huang, Yaoxing ; Shapiro, Lawrence ; Ho, David D.
Subjects: Adult ; Aged ; Animals ; Antibodies, Monoclonal - immunology ; Antibodies, Neutralizing - immunology ; Antibodies, Viral - immunology ; antibody ; Brief Report ; Chlorocebus aethiops ; convalescent plasma ; COVID-19 Vaccines - immunology ; Female ; HEK293 Cells ; Humans ; Male ; Middle Aged ; mutation ; neutralization ; Neutralization Tests ; NTD ; P.1 ; RBD ; SARS-CoV-2 ; SARS-CoV-2 - immunology ; Spike Glycoprotein, Coronavirus - chemistry ; Spike Glycoprotein, Coronavirus - genetics ; vaccine ; variant ; Vero Cells
Is Part Of: Cell host & microbe, 2021-05, Vol.29 (5), p.747-751.e4
Description: 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. [Display omitted] •P.1 is refractory to multiple neutralizing mAbs, including three out of the four with EUA•P.1 is relatively resistant to neutralization by convalescent plasma and vaccinee sera•Cryo-EM structure of P.1 spike trimer reveals exclusively one-RBD-up conformation Wang et al. report that an emergent SARS-CoV-2 variant, P.1, is relatively resistant to neutralization by multiple therapeutic monoclonal antibodies, convalescent plasma, and vaccinee sera. The cryoelectron microscopy structure reveals the P.1 trimer to adopt exclusively a conformation with one of the receptor-binding domains in the “up” position.
Publisher: United States: Elsevier Inc
Language: English
Identifier: ISSN: 1931-3128
EISSN: 1934-6069
DOI: 10.1016/j.chom.2021.04.007
PMID: 33887205
Source: Cell Press Free Archives
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Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization

2021 Elsevier Inc. ;Copyright © 2021 Elsevier Inc. All rights reserved. ;2021 Elsevier Inc. 2021 Elsevier Inc. ;ISSN: 1931-3128 ;EISSN: 1934-6069 ;DOI: 10.1016/j.chom.2021.04.007 ;PMID: 33887205

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