Structures of protective antibodies reveal sites of vulnerability on Ebola virus

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Abstract
Significance: Ebola virus causes lethal hemorrhagic fever, and the current 2014 outbreak in western Africa is the largest on record to date. No vaccines or therapeutics are yet approved for human use. Therapeutic antibody cocktails, however, have shown efficacy against otherwise lethal Ebola virus infection and show significant promise for eventual human use. Here we provide structures of every mAb in the ZMapp cocktail, as well as additional antibodies from the MB-003 and ZMAb cocktails from which ZMapp was derived, each in complex with the Ebola glycoprotein. The set of structures illustrates sites of vulnerability of Ebola virus, and importantly, provides a roadmap to determine their mechanism of protection and for ongoing selection and improvement of immunotherapeutic cocktails against the filoviruses.
Funding Information
  • HHS | National Institutes of Health (NIH) (R01AI067927)
  • HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) (U19AI109762)