7NEG

Crystal structure of the N501Y mutant receptor binding domain of SARS-CoV-2 Spike glycoprotein in complex with COVOX-269 Fab

Summary for 7NEG

• Entry DOI: 10.2210/pdb7neg/pdb
• Descriptor: Antibody COVOX-269 Fab heavy chain, Antibody COVOX-269 Fab light chain, Surface glycoprotein, ... (7 entities in total)
• Functional Keywords: sars-cov-2 b.1.1.7 variant, n501y mutation, antibody, receptor-binding-domain, spike, neutralisation, viral protein/immune system, viral protein-immune system complex
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 71838.14

Authors

Zhou, D.,Ren, J.,Stuart, D. (deposition date: 2021-02-04, release date: 2021-03-03, Last modification date: 2024-01-31)

Primary citation

Supasa, P.,Zhou, D.,Dejnirattisai, W.,Liu, C.,Mentzer, A.J.,Ginn, H.M.,Zhao, Y.,Duyvesteyn, H.M.E.,Nutalai, R.,Tuekprakhon, A.,Wang, B.,Paesen, G.C.,Slon-Campos, J.,Lopez-Camacho, C.,Hallis, B.,Coombes, N.,Bewley, K.R.,Charlton, S.,Walter, T.S.,Barnes, E.,Dunachie, S.J.,Skelly, D.,Lumley, S.F.,Baker, N.,Shaik, I.,Humphries, H.E.,Godwin, K.,Gent, N.,Sienkiewicz, A.,Dold, C.,Levin, R.,Dong, T.,Pollard, A.J.,Knight, J.C.,Klenerman, P.,Crook, D.,Lambe, T.,Clutterbuck, E.,Bibi, S.,Flaxman, A.,Bittaye, M.,Belij-Rammerstorfer, S.,Gilbert, S.,Hall, D.R.,Williams, M.A.,Paterson, N.G.,James, W.,Carroll, M.W.,Fry, E.E.,Mongkolsapaya, J.,Ren, J.,Stuart, D.I.,Screaton, G.R.
Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera.
Cell, 184:2201-, 2021

PubMed Abstract: SARS-CoV-2 has caused over 2 million deaths in little over a year. Vaccines are being deployed at scale, aiming to generate responses against the virus spike. The scale of the pandemic and error-prone virus replication is leading to the appearance of mutant viruses and potentially escape from antibody responses. Variant B.1.1.7, now dominant in the UK, with increased transmission, harbors 9 amino acid changes in the spike, including N501Y in the ACE2 interacting surface. We examine the ability of B.1.1.7 to evade antibody responses elicited by natural SARS-CoV-2 infection or vaccination. We map the impact of N501Y by structure/function analysis of a large panel of well-characterized monoclonal antibodies. B.1.1.7 is harder to neutralize than parental virus, compromising neutralization by some members of a major class of public antibodies through light-chain contacts with residue 501. However, widespread escape from monoclonal antibodies or antibody responses generated by natural infection or vaccination was not observed.

PubMed: 33743891
DOI: 10.1016/j.cell.2021.02.033

Experimental method

X-RAY DIFFRACTION (2.19 Å)