7BZ5

Structure of COVID-19 virus spike receptor-binding domain complexed with a neutralizing antibody

Summary for 7BZ5

• Entry DOI: 10.2210/pdb7bz5/pdb
• Descriptor: Spike protein S1, Heavy chain of B38, Light chain of B38, ... (5 entities in total)
• Functional Keywords: covid-19 antibody, viral protein, viral protein-immune system complex, viral protein/immune system
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV); More
• Total number of polymer chains: 3
• Total formula weight: 73360.00

Authors

Wu, Y.,Qi, J.,Gao, F. (deposition date: 2020-04-26, release date: 2020-05-13, Last modification date: 2024-10-30)

Primary citation

Wu, Y.,Wang, F.,Shen, C.,Peng, W.,Li, D.,Zhao, C.,Li, Z.,Li, S.,Bi, Y.,Yang, Y.,Gong, Y.,Xiao, H.,Fan, Z.,Tan, S.,Wu, G.,Tan, W.,Lu, X.,Fan, C.,Wang, Q.,Liu, Y.,Zhang, C.,Qi, J.,Gao, G.F.,Gao, F.,Liu, L.
A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2.
Science, 368:1274-1278, 2020

PubMed Abstract: Neutralizing antibodies could potentially be used as antivirals against the coronavirus disease 2019 (COVID-19) pandemic. Here, we report isolation of four human-origin monoclonal antibodies from a convalescent patient, all of which display neutralization abilities. The antibodies B38 and H4 block binding between the spike glycoprotein receptor binding domain (RBD) of the virus and the cellular receptor angiotensin-converting enzyme 2 (ACE2). A competition assay indicated different epitopes on the RBD for these two antibodies, making them a potentially promising virus-targeting monoclonal antibody pair for avoiding immune escape in future clinical applications. Moreover, a therapeutic study in a mouse model validated that these antibodies can reduce virus titers in infected lungs. The RBD-B38 complex structure revealed that most residues on the epitope overlap with the RBD-ACE2 binding interface, explaining the blocking effect and neutralizing capacity. Our results highlight the promise of antibody-based therapeutics and provide a structural basis for rational vaccine design.

PubMed: 32404477
DOI: 10.1126/science.abc2241

Experimental method

X-RAY DIFFRACTION (1.84 Å)