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A shared structural solution for neutralizing ebolaviruses

João M Dias1, Ana I Kuehne, Dafna M Abelson

  • 1Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA.

Nature Structural & Molecular Biology
|November 22, 2011
PubMed

Insights

A new antibody, 16F6, neutralizes the lethal Sudan virus by targeting its glycoprotein. This discovery offers a potential therapeutic strategy against Ebolavirus infections.

Area of Science:

  • Virology
  • Immunology
  • Structural Biology

Background:

  • Sudan virus, an Ebolavirus species, poses a significant lethal threat.
  • No effective monoclonal antibodies were previously known to neutralize Sudan virus.

Purpose of the Study:

  • To identify and characterize a neutralizing antibody against Sudan virus.
  • To elucidate the structural basis of Sudan virus neutralization by antibodies.

Main Methods:

  • Description of antibody 16F6 isolation and characterization.
  • Determination of the crystal structure of Sudan virus glycoprotein in complex with antibody 16F6.

Main Results:

  • Antibody 16F6 was found to neutralize Sudan virus.
  • The structure revealed that 16F6 binds to the viral glycoprotein.
  • The epitope recognized by 16F6 overlaps with that of antibody KZ52, another antibody targeting the GP(1,2) core.
  • Both 16F6 and KZ52 antibodies neutralize at a post-internalization step, likely during fusion.

Conclusions:

  • Antibody 16F6 represents a novel neutralizing agent against Sudan virus.
  • The overlapping epitope suggests a critical vulnerability in the Ebolavirus glycoprotein.
  • Understanding this neutralization mechanism may inform the development of broader Ebolavirus therapeutics.

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