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A shared structural solution for neutralizing ebolaviruses.

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.

SUBMITTER: Dias JM

PROVIDER: S-EPMC3230659 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature

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A shared structural solution for neutralizing ebolaviruses.

Dias João M JM Kuehne Ana I AI Abelson Dafna M DM Bale Shridhar S Wong Anthony C AC Halfmann Peter P Muhammad Majidat A MA Fusco Marnie L ML Zak Samantha E SE Kang Eugene E Kawaoka Yoshihiro Y Chandran Kartik K Dye John M JM Saphire Erica Ollmann EO

Nature structural & molecular biology 20111120 12

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. ...[more]

PMID: 22101933

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