Neutralizing ebolavirus: structural insights into the envelope glycoprotein and antibodies targeted against it

Curr Opin Struct Biol. 2009 Aug;19(4):408-17. doi: 10.1016/j.sbi.2009.05.004. Epub 2009 Jun 24.

Abstract

The ebolavirus (EBOV) envelope glycoprotein (GP) is solely responsible for viral attachment to, fusion with, and entry of new host cells, and consequently is a major target of vaccine design efforts. Recently determined crystal structures of key antibodies in complex with their EBOV epitopes have provided insights into the molecular architecture of GP and defined likely hotspots for viral neutralization. In this review, we discuss the structural basis for antibody-mediated neutralization of ebolavirus and its implications for novel therapeutic or vaccine strategies.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Antibodies, Neutralizing / immunology*
  • Antibodies, Viral / immunology*
  • Ebolavirus / immunology*
  • Ebolavirus / physiology
  • Humans
  • Mucins / chemistry
  • Protein Structure, Tertiary
  • Viral Envelope Proteins / chemistry*
  • Viral Envelope Proteins / immunology*
  • Viral Envelope Proteins / metabolism
  • Virus Internalization

Substances

  • Antibodies, Neutralizing
  • Antibodies, Viral
  • Mucins
  • Viral Envelope Proteins