Viral membrane fusion

Nat Struct Mol Biol. 2008 Jul;15(7):690-8. doi: 10.1038/nsmb.1456.


Infection by viruses having lipid-bilayer envelopes proceeds through fusion of the viral membrane with a membrane of the target cell. Viral 'fusion proteins' facilitate this process. They vary greatly in structure, but all seem to have a common mechanism of action, in which a ligand-triggered, large-scale conformational change in the fusion protein is coupled to apposition and merger of the two bilayers. We describe three examples--the influenza virus hemagglutinin, the flavivirus E protein and the vesicular stomatitis virus G protein--in some detail, to illustrate the ways in which different structures have evolved to implement this common mechanism. Fusion inhibitors can be effective antiviral agents.

Publication types

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

MeSH terms

  • Animals
  • Hemagglutinin Glycoproteins, Influenza Virus / chemistry
  • Hemagglutinin Glycoproteins, Influenza Virus / metabolism
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / metabolism
  • Viral Envelope Proteins / chemistry
  • Viral Envelope Proteins / metabolism
  • Virus Activation
  • Virus Internalization*


  • G protein, vesicular stomatitis virus
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Membrane Glycoproteins
  • Viral Envelope Proteins
  • glycoprotein E, Flavivirus