| Literature DB >> 25723164 |
Andrew I Flyak1, Philipp A Ilinykh2, Charles D Murin3, Tania Garron2, Xiaoli Shen2, Marnie L Fusco4, Takao Hashiguchi4, Zachary A Bornholdt4, James C Slaughter5, Gopal Sapparapu6, Curtis Klages2, Thomas G Ksiazek2, Andrew B Ward7, Erica Ollmann Saphire8, Alexander Bukreyev2, James E Crowe9.
Abstract
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.Entities:
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Year: 2015 PMID： 25723164 PMCID： PMC4344968 DOI： 10.1016/j.cell.2015.01.031
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582