A Shared Structural Solution for Neutralizing Ebolaviruses

Sudan virus (genus ebolavirus) is lethal, yet no monoclonal antibody is known to neutralize it. Here we 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 antibod...

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Detalles Bibliográficos
Autores principales: Dias, João M., Kuehne, Ana I., Abelson, Dafna M., Bale, Shridhar, Wong, Anthony C., Halfmann, Peter, Muhammad, Majidat A., Fusco, Marnie L., Zak, Samantha E., Kang, Eugene, Kawaoka, Yoshihiro, Chandran, Kartik, Dye, John M., Saphire, Erica Ollmann
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3230659/
https://www.ncbi.nlm.nih.gov/pubmed/22101933
http://dx.doi.org/10.1038/nsmb.2150
Descripción
Sumario:Sudan virus (genus ebolavirus) is lethal, yet no monoclonal antibody is known to neutralize it. Here we 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. Further, both antibodies against this key GP1–GP2-bridging epitope neutralize at a post-internalization step, likely fusion.

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