Mechanism of human antibody-mediated neutralization of Marburg virus.

Flyak AI, Ilinykh PA, Murin CD, Garron T, Shen X, Fusco ML, Hashiguchi T, Bornholdt ZA, Slaughter JC, Sapparapu G, Klages C, Ksiazek TG, Ward AB, Saphire EO, Bukreyev A, Crowe JE
Cell. 2015 160 (5): 893-903

PMID: 25723164 · PMCID: PMC4344968 · DOI:10.1016/j.cell.2015.01.031

The mechanisms by which neutralizing antibodies inhibit Marburg virus (MARV) are not known. We isolated a panel of neutralizing antibodies from a human MARV survivor that bind to MARV glycoprotein (GP) and compete for binding to a single major antigenic site. Remarkably, several of the antibodies also bind to Ebola virus (EBOV) GP. Single-particle EM structures of antibody-GP complexes reveal that all of the neutralizing antibodies bind to MARV GP at or near the predicted region of the receptor-binding site. The presence of the glycan cap or mucin-like domain blocks binding of neutralizing antibodies to EBOV GP, but not to MARV GP. The data suggest that MARV-neutralizing antibodies inhibit virus by binding to infectious virions at the exposed MARV receptor-binding site, revealing a mechanism of filovirus inhibition.

Copyright © 2015 Elsevier Inc. All rights reserved.

MeSH Terms (16)

Adult Animals Antibodies, Monoclonal Antibodies, Neutralizing Antibodies, Viral Antigen-Antibody Complex B-Lymphocytes Female Humans Immunoglobulin Fab Fragments Marburgvirus Marburg Virus Disease Models, Molecular Mutation Protein Structure, Tertiary Viral Envelope Proteins

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