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 DOI | 10.2210/pdb7m8k/pdb |
EMDB information | 23718 |
Descriptor | Spike 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 Keywords | spike glycoprotein, viral protein |
Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) |
Total number of polymer chains | 3 |
Total formula weight | 429062.33 |
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 citation | Wang, 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: 33887205DOI: 10.1016/j.chom.2021.04.007 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY |
Structure validation
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