• Pengfei Wang, Ryan G Casner, Manoj S Nair, Maple Wang, Jian Yu, Gabriele Cerutti, Lihong Liu, Peter D Kwong, Yaoxing Huang, Lawrence Shapiro, and David D Ho.
• Aaron Diamond AIDS Research Center, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032, USA. Electronic address: pw2517@cumc.columbia.edu.
• Cell Host Microbe. 2021 May 12; 29 (5): 747-751.e4.

AbstractThe 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.Copyright © 2021 Elsevier Inc. All rights reserved.

34 keywords...

hide…