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7M8K

Cryo-EM structure of Brazil (P.1) SARS-CoV-2 spike glycoprotein variant in the prefusion state (1 RBD up)

Summary for 7M8K
Entry DOI10.2210/pdb7m8k/pdb
EMDB information23718
DescriptorSpike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordsspike glycoprotein, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
Total number of polymer chains3
Total formula weight429062.33
Authors
Casner, R.G.,Cerutti, G.,Shapiro, L.,Ho, D.D. (deposition date: 2021-03-29, release date: 2021-05-05, Last modification date: 2024-11-13)
Primary citationWang, P.,Casner, R.G.,Nair, M.S.,Wang, M.,Yu, J.,Cerutti, G.,Liu, L.,Kwong, P.D.,Huang, Y.,Shapiro, L.,Ho, D.D.
Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization.
Cell Host Microbe, 29:747-, 2021
Cited by
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 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.
PubMed: 33887205
DOI: 10.1016/j.chom.2021.04.007
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY
Structure validation

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