Stuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entry

Curr Opin Virol. 2013 Feb;3(1):13-9. doi: 10.1016/j.coviro.2012.10.005. Epub 2012 Oct 26.

Abstract

Enveloped viruses enter cells by fusing the viral and cellular membranes, and most use a single viral envelope protein that combines receptor-binding and fusogenic functions. In herpesviruses, these functions are distributed among multiple proteins: the conserved fusion protein gB, various non-conserved receptor-binding proteins, and the conserved gH/gL heterodimer that curiously lacks an apparent counterpart in other enveloped viruses. Recent structural studies of gH/gL from HSV-2 and EBV revealed a unique complex with no structural or functional similarity to other viral proteins. Here we analyzed gH/gL structures and highlighted important functional regions. We propose that gH/gL functions as an adaptor that transmits the triggering signals from various non-conserved inputs to the highly conserved fusion protein gB.

Publication types

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

MeSH terms

  • Herpesvirus 2, Human / chemistry*
  • Herpesvirus 2, Human / physiology
  • Herpesvirus 4, Human / chemistry*
  • Herpesvirus 4, Human / physiology
  • Humans
  • Models, Biological
  • Models, Molecular
  • Protein Conformation
  • Protein Multimerization*
  • Viral Envelope Proteins / chemistry*
  • Viral Envelope Proteins / metabolism*
  • Virus Internalization*

Substances

  • Viral Envelope Proteins