A shared structural solution for neutralizing ebolaviruses.

Authors :: 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
Source :: Nature Structural & Molecular Biology; Dec2011, Vol. 18 Issue 12, p1424-1427, 4p, 3 Diagrams
Publication Year :: 2011
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<subscript>1,2</subscript> core to be visualized to date. Furthermore, both antibodies against this crucial epitope bridging GP1-GP2 neutralize at a post-internalization step-probably fusion. [ABSTRACT FROM AUTHOR]