A shared structural solution for neutralizing ebolaviruses

João M. Dias, Ana I. Kuehne, Dafna M. Abelson, Shridhar Bale, Anthony C. Wong, Peter Halfmann, Majidat A. Muhammad, Marnie L. Fusco, Samantha E. Zak, Eugene Kang, Yoshihiro Kawaoka, Kartik Chandran, John M. Dye, Erica Ollmann Saphire

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90 Scopus citations

Abstract

Sudan virus (genus Ebolavirus) is lethal, yet no monoclonal antibody is known to neutralize it. We here describe antibody 16F6 that neutralizes Sudan virus and present its structure bound to the trimeric viral glycoprotein. Unexpectedly, the 16F6 epitope overlaps that of KZ52, the only other antibody against the GP 1,2 core to be visualized to date. Furthermore, both antibodies against this crucial epitope bridging GP1-GP2 neutralize at a post-internalization step-probably fusion.

Original languageEnglish (US)
Pages (from-to)1424-1427
Number of pages4
JournalNature Structural and Molecular Biology
Volume18
Issue number12
DOIs
StatePublished - Dec 1 2011

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ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Dias, J. M., Kuehne, A. I., Abelson, D. M., Bale, S., Wong, A. C., Halfmann, P., Muhammad, M. A., Fusco, M. L., Zak, S. E., Kang, E., Kawaoka, Y., Chandran, K., Dye, J. M., & Saphire, E. O. (2011). A shared structural solution for neutralizing ebolaviruses. Nature Structural and Molecular Biology, 18(12), 1424-1427. https://doi.org/10.1038/nsmb.2150