7LOP

Crystal structure of SARS-CoV-2 receptor binding domain in complex with antibodies CV05-163 and CR3022

Summary for 7LOP

• Entry DOI: 10.2210/pdb7lop/pdb
• Descriptor: CR3022 Fab heavy chain, CR3022 Fab light chain, Spike protein S1, ... (7 entities in total)
• Functional Keywords: sars-cov-2, receptor binding domain, coronavirus, covid-19, antibody, fab, immune system, viral protein-immune system complex, viral protein/immune system
• Biological source: Homo sapiens; More
• Total number of polymer chains: 10
• Total formula weight: 243794.73

Authors

Yuan, M.,Zhu, X.,Wilson, I.A. (deposition date: 2021-02-10, release date: 2021-03-03, Last modification date: 2024-10-23)

Primary citation

Yuan, M.,Huang, D.,Lee, C.D.,Wu, N.C.,Jackson, A.M.,Zhu, X.,Liu, H.,Peng, L.,van Gils, M.J.,Sanders, R.W.,Burton, D.R.,Reincke, S.M.,Pruss, H.,Kreye, J.,Nemazee, D.,Ward, A.B.,Wilson, I.A.
Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants.
Science, 373:818-823, 2021

PubMed Abstract: Neutralizing antibodies (nAbs) elicited against the receptor binding site (RBS) of the spike protein of wild-type severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are generally less effective against recent variants of concern. RBS residues Glu, Lys, and Asn are mutated in variants first described in South Africa (B.1.351) and Brazil (P.1). We analyzed their effects on angiotensin-converting enzyme 2 binding, as well as the effects of two of these mutations (K417N and E484K) on nAbs isolated from COVID-19 patients. Binding and neutralization of the two most frequently elicited antibody families (IGHV3-53/3-66 and IGHV1-2), which can both bind the RBS in alternative binding modes, are abrogated by K417N, E484K, or both. These effects can be structurally explained by their extensive interactions with RBS nAbs. However, nAbs to the more conserved, cross-neutralizing CR3022 and S309 sites were largely unaffected. The results have implications for next-generation vaccines and antibody therapies.

PubMed: 34016740
DOI: 10.1126/science.abh1139

Experimental method

X-RAY DIFFRACTION (2.246 Å)