Analysis of a Therapeutic Antibody Cocktail Reveals Determinants for Cooperative and Broad Ebolavirus Neutralization

Pavlo Gilchuk, Charles D. Murin, Jacob C. Milligan, Robert W. Cross, Chad E. Mire, Philipp A. Ilinykh, Kai Huang, Natalia Kuzmina, Pilar X. Altman, Sean Hui, Bronwyn M. Gunn, Aubrey L. Bryan, Edgar Davidson, Benjamin J. Doranz, Hannah L. Turner, Tanwee Alkutkar, Robin Flinko, Chiara Orlandi, Robert Carnahan, Rachel NargiRobin G. Bombardi, Megan E. Vodzak, Sheng Li, Adaora Okoli, Morris Ibeawuchi, Benjamin Ohiaeri, George K. Lewis, Galit Alter, Alexander Bukreyev, Erica Ollmann Saphire, Thomas W. Geisbert, Andrew B. Ward, James E. Crowe

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Cooperative interactions of monoclonal antibodies (mAbs) with viral antigens are poorly understood. Gilchuk et al. perform structural and functional analysis of cooperativity in a cocktail of two human mAbs, recognizing major epitopes of ebolavirus glycoprotein (GP), and define cooperative binding of the GP as a mechanism for enhanced ebolavirus neutralization.

Original languageEnglish (US)
Pages (from-to)388-403.e12
JournalImmunity
Volume52
Issue number2
DOIs
StatePublished - Feb 18 2020

Keywords

  • Ebolavirus
  • antibody synergy
  • antibody therapeutics
  • cooperative neutralization
  • ebolavirus infection
  • epitope mapping
  • glycoprotein
  • molecular mimicry
  • neutralizing antibodies
  • viral antibodies

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Infectious Diseases

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