7ORB

Crystal structure of the L452R mutant receptor binding domain of SARS-CoV-2 Spike glycoprotein in complex with COVOX-75 and COVOX-253 Fabs

Summary for 7ORB

• Entry DOI: 10.2210/pdb7orb/pdb
• Descriptor: Spike protein S1, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (16 entities in total)
• Functional Keywords: sars-cov-2 b.1.1.7 variant, b.1.351 variant, p.1 variant, b.1.617 variant, antibody, receptor-binding-domain, spike, neutralisation, viral protein/immune system, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2); More
• Total number of polymer chains: 10
• Total formula weight: 243812.59

Authors

Zhou, D.,Ren, J.,Stuart, D.I. (deposition date: 2021-06-04, release date: 2021-07-07, Last modification date: 2024-01-31)

Primary citation

Liu, C.,Ginn, H.M.,Dejnirattisai, W.,Supasa, P.,Wang, B.,Tuekprakhon, A.,Nutalai, R.,Zhou, D.,Mentzer, A.J.,Zhao, Y.,Duyvesteyn, H.M.E.,Lopez-Camacho, C.,Slon-Campos, J.,Walter, T.S.,Skelly, D.,Johnson, S.A.,Ritter, T.G.,Mason, C.,Costa Clemens, S.A.,Gomes Naveca, F.,Nascimento, V.,Nascimento, F.,Fernandes da Costa, C.,Resende, P.C.,Pauvolid-Correa, A.,Siqueira, M.M.,Dold, C.,Temperton, N.,Dong, T.,Pollard, A.J.,Knight, J.C.,Crook, D.,Lambe, T.,Clutterbuck, E.,Bibi, S.,Flaxman, A.,Bittaye, M.,Belij-Rammerstorfer, S.,Gilbert, S.C.,Malik, T.,Carroll, M.W.,Klenerman, P.,Barnes, E.,Dunachie, S.J.,Baillie, V.,Serafin, N.,Ditse, Z.,Da Silva, K.,Paterson, N.G.,Williams, M.A.,Hall, D.R.,Madhi, S.,Nunes, M.C.,Goulder, P.,Fry, E.E.,Mongkolsapaya, J.,Ren, J.,Stuart, D.I.,Screaton, G.R.
Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum.
Cell, 184:4220-4236.e13, 2021

PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has undergone progressive change, with variants conferring advantage rapidly becoming dominant lineages, e.g., B.1.617. With apparent increased transmissibility, variant B.1.617.2 has contributed to the current wave of infection ravaging the Indian subcontinent and has been designated a variant of concern in the United Kingdom. Here we study the ability of monoclonal antibodies and convalescent and vaccine sera to neutralize B.1.617.1 and B.1.617.2, complement this with structural analyses of Fab/receptor binding domain (RBD) complexes, and map the antigenic space of current variants. Neutralization of both viruses is reduced compared with ancestral Wuhan-related strains, but there is no evidence of widespread antibody escape as seen with B.1.351. However, B.1.351 and P.1 sera showed markedly more reduction in neutralization of B.1.617.2, suggesting that individuals infected previously by these variants may be more susceptible to reinfection by B.1.617.2. This observation provides important new insights for immunization policy with future variant vaccines in non-immune populations.

PubMed: 34242578
DOI: 10.1016/j.cell.2021.06.020

Experimental method

X-RAY DIFFRACTION (2.5 Å)