6XDG

Complex of SARS-CoV-2 receptor binding domain with the Fab fragments of two neutralizing antibodies

Summary for 6XDG

• Entry DOI: 10.2210/pdb6xdg/pdb
• EMDB information: 22137
• Descriptor: Spike protein S1, REGN10933 antibody Fab fragment light chain, REGN10933 antibody Fab fragment heavy chain, ... (6 entities in total)
• Functional Keywords: sars-cov-2, therapeutic antibody, antiviral, 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: 5
• Total formula weight: 123517.56

Authors

Franklin, M.C.,Saotome, K.,Romero Hernandez, A.,Zhou, Y. (deposition date: 2020-06-10, release date: 2020-06-24, Last modification date: 2024-11-13)

Primary citation

Hansen, J.,Baum, A.,Pascal, K.E.,Russo, V.,Giordano, S.,Wloga, E.,Fulton, B.O.,Yan, Y.,Koon, K.,Patel, K.,Chung, K.M.,Hermann, A.,Ullman, E.,Cruz, J.,Rafique, A.,Huang, T.,Fairhurst, J.,Libertiny, C.,Malbec, M.,Lee, W.Y.,Welsh, R.,Farr, G.,Pennington, S.,Deshpande, D.,Cheng, J.,Watty, A.,Bouffard, P.,Babb, R.,Levenkova, N.,Chen, C.,Zhang, B.,Romero Hernandez, A.,Saotome, K.,Zhou, Y.,Franklin, M.,Sivapalasingam, S.,Lye, D.C.,Weston, S.,Logue, J.,Haupt, R.,Frieman, M.,Chen, G.,Olson, W.,Murphy, A.J.,Stahl, N.,Yancopoulos, G.D.,Kyratsous, C.A.
Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail.
Science, 369:1010-1014, 2020

PubMed Abstract: Neutralizing antibodies have become an important tool in treating infectious diseases. Recently, two separate approaches yielded successful antibody treatments for Ebola-one from genetically humanized mice and the other from a human survivor. Here, we describe parallel efforts using both humanized mice and convalescent patients to generate antibodies against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein, which yielded a large collection of fully human antibodies that were characterized for binding, neutralization, and three-dimensional structure. On the basis of these criteria, we selected pairs of highly potent individual antibodies that simultaneously bind the receptor binding domain of the spike protein, thereby providing ideal partners for a therapeutic antibody cocktail that aims to decrease the potential for virus escape mutants that might arise in response to selective pressure from a single-antibody treatment.

PubMed: 32540901
DOI: 10.1126/science.abd0827

Experimental method

ELECTRON MICROSCOPY (3.9 Å)