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Title | Mechanism of human antibody-mediated neutralization of Marburg virus. |
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Journal, issue, pages | Cell, Vol. 160, Issue 5, Page 893-903, Year 2015 |
Publish date | Feb 26, 2015 |
Authors | Andrew I Flyak / Philipp A Ilinykh / Charles D Murin / Tania Garron / Xiaoli Shen / Marnie L Fusco / Takao Hashiguchi / Zachary A Bornholdt / James C Slaughter / Gopal Sapparapu / Curtis Klages / Thomas G Ksiazek / Andrew B Ward / Erica Ollmann Saphire / Alexander Bukreyev / James E Crowe / |
PubMed 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 ...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. |
External links | Cell / PubMed:25723164 / PubMed Central |
Methods | EM (single particle) |
Resolution | 22.0 - 27.0 Å |
Structure data | EMDB-6232: EMDB-6233: EMDB-6234: EMDB-6235: EMDB-6236: EMDB-6237: EMDB-6238: |
Source |
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