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7SN3

Structure of human SARS-CoV-2 spike glycoprotein trimer bound by neutralizing antibody C1C-A3 Fab (variable region)

Summary for 7SN3
Entry DOI10.2210/pdb7sn3/pdb
Related7SN2
EMDB information25209 25210
DescriptorSpike glycoprotein, neutralizing antibody C1C-A3 heavy chain variable region, neutralizing antibody C1C-A3 light chain variable region, ... (5 entities in total)
Functional Keywordscovid-19, sars-cov-2, neutralizing antibody, neutralization escape, immune system, viral protein-immune system complex, viral protein/immune system
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
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Total number of polymer chains9
Total formula weight594046.74
Authors
Pan, J.,Abraham, J.,Shankar, S. (deposition date: 2021-10-27, release date: 2021-12-08, Last modification date: 2024-10-09)
Primary citationNabel, K.G.,Clark, S.A.,Shankar, S.,Pan, J.,Clark, L.E.,Yang, P.,Coscia, A.,McKay, L.G.A.,Varnum, H.H.,Brusic, V.,Tolan, N.V.,Zhou, G.,Desjardins, M.,Turbett, S.E.,Kanjilal, S.,Sherman, A.C.,Dighe, A.,LaRocque, R.C.,Ryan, E.T.,Tylek, C.,Cohen-Solal, J.F.,Darcy, A.T.,Tavella, D.,Clabbers, A.,Fan, Y.,Griffiths, A.,Correia, I.R.,Seagal, J.,Baden, L.R.,Charles, R.C.,Abraham, J.
Structural basis for continued antibody evasion by the SARS-CoV-2 receptor binding domain.
Science, 375:eabl6251-eabl6251, 2022
Cited by
PubMed Abstract: Many studies have examined the impact of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants on neutralizing antibody activity after they have become dominant strains. Here, we evaluate the consequences of further viral evolution. We demonstrate mechanisms through which the SARS-CoV-2 receptor binding domain (RBD) can tolerate large numbers of simultaneous antibody escape mutations and show that pseudotypes containing up to seven mutations, as opposed to the one to three found in previously studied variants of concern, are more resistant to neutralization by therapeutic antibodies and serum from vaccine recipients. We identify an antibody that binds the RBD core to neutralize pseudotypes for all tested variants but show that the RBD can acquire an N-linked glycan to escape neutralization. Our findings portend continued emergence of escape variants as SARS-CoV-2 adapts to humans.
PubMed: 34855508
DOI: 10.1126/science.abl6251
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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