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8EQF

cryoEM structure of a broadly neutralizing anti-SARS-CoV-2 antibody STI-9167

Summary for 8EQF
Entry DOI10.2210/pdb8eqf/pdb
EMDB information28537 29227
DescriptorSpike protein S1, Fab heavy chain, Fab light chain, ... (4 entities in total)
Functional Keywordsantibody, sars-cov-2, immune system
Biological sourceSevere acute respiratory syndrome coronavirus 2
More
Total number of polymer chains3
Total formula weight47777.22
Authors
Bajic, G. (deposition date: 2022-10-07, release date: 2023-10-11, Last modification date: 2025-05-21)
Primary citationAtanasoff, K.E.,Brambilla, L.,Adelsberg, D.C.,Kowdle, S.,Stevens, C.S.,Slamanig, S.,Hung, C.T.,Fu, Y.,Lim, R.,Tran, L.,Allen, R.,Sun, W.,Duty, J.A.,Bajic, G.,Lee, B.,Tortorella, D.
An in vitro experimental pipeline to characterize the epitope of a SARS-CoV-2 neutralizing antibody.
Mbio, 15:e0247723-e0247723, 2024
Cited by
PubMed Abstract: The COVID-19 pandemic remains a significant public health concern for the global population; the development and characterization of therapeutics, especially ones that are broadly effective, will continue to be essential as severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2) variants emerge. Neutralizing monoclonal antibodies remain an effective therapeutic strategy to prevent virus infection and spread so long as they recognize and interact with circulating variants. The epitope and binding specificity of a neutralizing anti-SARS-CoV-2 Spike receptor-binding domain antibody clone against many SARS-CoV-2 variants of concern were characterized by generating antibody-resistant virions coupled with cryo-EM structural analysis and VSV-spike neutralization studies. This workflow can serve to predict the efficacy of antibody therapeutics against emerging variants and inform the design of therapeutics and vaccines.
PubMed: 38054729
DOI: 10.1128/mbio.02477-23
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.16 Å)
Structure validation

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