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Increased Resistance of SARS-CoV-2 Variant P.1 to Antibody Neutralization.

ABSTRACT: The relative resistance of SARS-CoV-2 variants B.1.1.7 and B.1.351 to antibody neutralization has been described recently. We now 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 (3.4 fold) and vaccinee sera (3.8-4.8 fold). The cryo-electron microscopy structure of a soluble prefusion-stabilized spike reveals the P.1 trimer to adopt exclusively a conformation in which one of the receptor-binding domains is in the "up" position, with the functional impact of mutations appearing to arise from local changes instead of global conformational alterations. The P.1 variant threatens current antibody therapies but less so the protective efficacy of our vaccines.

SUBMITTER: Wang P

PROVIDER: S-EPMC7941628 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature

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Increased Resistance of SARS-CoV-2 Variant P.1 to Antibody Neutralization.

Wang Pengfei P Casner Ryan G RG Nair Manoj S MS Wang Maple M Yu Jian J Cerutti Gabriele G Liu Lihong L Kwong Peter D PD Huang Yaoxing Y Shapiro Lawrence L Ho David D DD

bioRxiv : the preprint server for biology 20210409

The relative resistance of SARS-CoV-2 variants B.1.1.7 and B.1.351 to antibody neutralization has been described recently. We now 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 (3.4 fold) and vaccinee sera (3.8-4.8 fold). The cryo-electron microscopy structure of a soluble prefusion-stabilized spike reveals the P.1 trimer to adopt exclusively a conformat ...[more]

PMID: 33688656

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