A shared structural solution for neutralizing ebolaviruses

Academic Article

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Overview

authors

• 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, Erica Ollmann

publication date

• 2011

journal

• Nature Structural & Molecular Biology  Journal

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.

subject areas

• Animals
• Antibodies, Monoclonal
• Antibodies, Neutralizing
• Crystallography, X-Ray
• Ebolavirus
• Epitopes
• HEK293 Cells
• Humans
• Mice
• Mice, Inbred BALB C
• Models, Immunological
• Models, Molecular
• Neutralization Tests
• Protein Structure, Tertiary
• Viral Fusion Proteins

Identity

PubMed Central ID

• PMC3230659

International Standard Serial Number (ISSN)

• 1545-9993

Digital Object Identifier (DOI)

• 10.1038/nsmb.2150

PubMed ID

• 22101933

Additional Document Info

start page

• 1424

end page

• 1427

volume

• 18

issue

• 12