Journal
CELL
Volume 160, Issue 5, Pages 893-903Publisher
CELL PRESS
DOI: 10.1016/j.cell.2015.01.031
Keywords
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Categories
Funding
- Defense Threat Reduction Agency [HDTRA1-13-1-0034]
- U.S. NIH [1U19AI109711, U19AI109762, R01AI089498, U01AI082156]
- NCRR [UL1 RR024975-01]
- National Center for Advancing Translational Sciences [UL1 TR000445-06]
- MEXT
- JSPS
- Uehara Memorial Foundation
- NIH [P30 CA68485, DK058404]
- Biomedical Technology Research Center program of the National Institute of General Medical Sciences [GM103310]
- NATIONAL CANCER INSTITUTE [P30CA068485] Funding Source: NIH RePORTER
- NATIONAL CENTER FOR ADVANCING TRANSLATIONAL SCIENCES [UL1TR000445] Funding Source: NIH RePORTER
- NATIONAL CENTER FOR RESEARCH RESOURCES [UL1RR024975] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [T32HL069765] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [U19AI109762, T32AI007244, R01AI089498, U01AI082156, U19AI109711] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [P30DK058404] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P41GM103310] Funding Source: NIH RePORTER
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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.
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