7SBU

Crystal structure of SARS-CoV-2 spike protein receptor-binding domain in complex with a highly potent antibody J08 Fab

Summary for 7SBU

• Entry DOI: 10.2210/pdb7sbu/pdb
• Descriptor: Spike protein S1, J08 Fab heavy chain, J08 Fab light chain, ... (6 entities in total)
• Functional Keywords: sars-cov-2, antibody, spike, coronavirus, covid-19, immune system, viral protein-immune system complex, neutralizing antibody, receptor binding domain
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2); More
• Total number of polymer chains: 3
• Total formula weight: 70691.96

Authors

Liu, H.,Wilson, I.A. (deposition date: 2021-09-25, release date: 2022-05-11, Last modification date: 2023-10-18)

Primary citation

Torres, J.L.,Ozorowski, G.,Andreano, E.,Liu, H.,Copps, J.,Piccini, G.,Donnici, L.,Conti, M.,Planchais, C.,Planas, D.,Manganaro, N.,Pantano, E.,Paciello, I.,Pileri, P.,Bruel, T.,Montomoli, E.,Mouquet, H.,Schwartz, O.,Sala, C.,De Francesco, R.,Wilson, I.A.,Rappuoli, R.,Ward, A.B.
Structural insights of a highly potent pan-neutralizing SARS-CoV-2 human monoclonal antibody.
Proc.Natl.Acad.Sci.USA, 119:e2120976119-e2120976119, 2022

PubMed Abstract: As the coronavirus disease 2019 (COVID-19) pandemic continues, there is a strong need for highly potent monoclonal antibodies (mAbs) that are resistant against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VoCs). Here, we evaluate the potency of the previously described mAb J08 against these variants using cell-based assays and delve into the molecular details of the binding interaction using cryoelectron microscopy (cryo-EM) and X-ray crystallography. We show that mAb J08 has low nanomolar affinity against most VoCs and binds high on the receptor binding domain (RBD) ridge, away from many VoC mutations. These findings further validate the phase II/III human clinical trial underway using mAb J08 as a monoclonal therapy.

PubMed: 35549549
DOI: 10.1073/pnas.2120976119

Experimental method

X-RAY DIFFRACTION (2.53 Å)