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7UAP

Structure of the SARS-CoV-2 S 6P trimer in complex with the neutralizing antibody Fab fragment, C1520

Summary for 7UAP
Entry DOI10.2210/pdb7uap/pdb
EMDB information26429
DescriptorSpike glycoprotein, C1520 Fab Heavy Chain, C1520 Fab Light Chain, ... (5 entities in total)
Functional Keywordssars-cov-2, n-terminal domain, ntd, neutralizing antibody, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2
More
Total number of polymer chains9
Total formula weight575740.04
Authors
Barnes, C.O. (deposition date: 2022-03-13, release date: 2022-04-27, Last modification date: 2024-11-13)
Primary citationWang, Z.,Muecksch, F.,Cho, A.,Gaebler, C.,Hoffmann, H.H.,Ramos, V.,Zong, S.,Cipolla, M.,Johnson, B.,Schmidt, F.,DaSilva, J.,Bednarski, E.,Ben Tanfous, T.,Raspe, R.,Yao, K.,Lee, Y.E.,Chen, T.,Turroja, M.,Milard, K.G.,Dizon, J.,Kaczynska, A.,Gazumyan, A.,Oliveira, T.Y.,Rice, C.M.,Caskey, M.,Bieniasz, P.D.,Hatziioannou, T.,Barnes, C.O.,Nussenzweig, M.C.
Analysis of memory B cells identifies conserved neutralizing epitopes on the N-terminal domain of variant SARS-Cov-2 spike proteins.
Immunity, 55:998-1012.e8, 2022
Cited by
PubMed Abstract: SARS-CoV-2 infection or vaccination produces neutralizing antibody responses that contribute to better clinical outcomes. The receptor-binding domain (RBD) and the N-terminal domain (NTD) of the spike trimer (S) constitute the two major neutralizing targets for antibodies. Here, we use NTD-specific probes to capture anti-NTD memory B cells in a longitudinal cohort of infected individuals, some of whom were vaccinated. We found 6 complementation groups of neutralizing antibodies. 58% targeted epitopes outside the NTD supersite, 58% neutralized either Gamma or Omicron, and 14% were broad neutralizers that also neutralized Omicron. Structural characterization revealed that broadly active antibodies targeted three epitopes outside the NTD supersite including a class that recognized both the NTD and SD2 domain. Rapid recruitment of memory B cells producing these antibodies into the plasma cell compartment upon re-infection likely contributes to the relatively benign course of subsequent infections with SARS-CoV-2 variants, including Omicron.
PubMed: 35447092
DOI: 10.1016/j.immuni.2022.04.003
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.8 Å)
Structure validation

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