7ZBU

CryoEM structure of SARS-CoV-2 spike monomer in complex with neutralising antibody P008_60

Summary for 7ZBU

• Entry DOI: 10.2210/pdb7zbu/pdb
• EMDB information: 14591
• Descriptor: Spike glycoprotein, P008_60 antibody, Heavy chain, P008_60 antibody, Light chain, ... (5 entities in total)
• Functional Keywords: covid-19, sars-cov-2, spike, neutralizing antibody, immunity, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2; More
• Total number of polymer chains: 3
• Total formula weight: 194171.36

Authors

Rosa, A.,Pye, V.E.,Cronin, N.,Cherepanov, P. (deposition date: 2022-03-24, release date: 2022-08-17, Last modification date: 2024-10-16)

Primary citation

Seow, J.,Khan, H.,Rosa, A.,Calvaresi, V.,Graham, C.,Pickering, S.,Pye, V.E.,Cronin, N.B.,Huettner, I.,Malim, M.H.,Politis, A.,Cherepanov, P.,Doores, K.J.
A neutralizing epitope on the SD1 domain of SARS-CoV-2 spike targeted following infection and vaccination.
Cell Rep, 40:111276-111276, 2022

PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike is the target for neutralizing antibodies elicited following both infection and vaccination. While extensive research has shown that the receptor binding domain (RBD) and, to a lesser extent, the N-terminal domain (NTD) are the predominant targets for neutralizing antibodies, identification of neutralizing epitopes beyond these regions is important for informing vaccine development and understanding antibody-mediated immune escape. Here, we identify a class of broadly neutralizing antibodies that bind an epitope on the spike subdomain 1 (SD1) and that have arisen from infection or vaccination. Using cryo-electron microscopy (cryo-EM) and hydrogen-deuterium exchange coupled to mass spectrometry (HDX-MS), we show that SD1-specific antibody P008_60 binds an epitope that is not accessible within the canonical prefusion states of the SARS-CoV-2 spike, suggesting a transient conformation of the viral glycoprotein that is vulnerable to neutralization.

PubMed: 35981534
DOI: 10.1016/j.celrep.2022.111276

Experimental method

ELECTRON MICROSCOPY (4.31 Å)