gH/gL supercomplexes at early stages of herpesvirus entry

Curr Opin Virol. 2016 Jun;18:1-8. doi: 10.1016/j.coviro.2016.01.010. Epub 2016 Feb 2.

Abstract

Membrane fusion during herpesvirus entry into host cells is a complex process where multiple glycoproteins interact to relay the triggering signal from a receptor-binding protein to the conserved fusogen gB through the conserved heterodimer gH/gL. Crystal structures of individual glycoproteins are available, yet high-order 'supercomplexes' have been elusive. Recent structures of complexes between gH/gL from human cytomegalovirus or Epstein-Barr virus and the receptor-binding proteins that form at early stages of herpesviral entry highlighted mechanisms that control tropism and revealed dynamic intermediate complexes containing gH/gL that may directly participate in membrane deformation and juxtaposition. Determining how the triggering signal reaches the fusogen gB represents the next frontier in structural biology of herpesvirus entry.

Publication types

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

MeSH terms

  • Cytomegalovirus / chemistry
  • Glycoproteins / chemistry
  • Glycoproteins / metabolism*
  • Herpesviridae / chemistry*
  • Herpesviridae / physiology*
  • Herpesvirus 2, Human / chemistry
  • Herpesvirus 4, Human / chemistry
  • Membrane Fusion
  • Microscopy, Electron
  • Multiprotein Complexes / chemistry
  • Multiprotein Complexes / metabolism*
  • Protein Binding
  • Viral Envelope Proteins / chemistry
  • Viral Envelope Proteins / metabolism*
  • Viral Tropism
  • Virus Internalization*

Substances

  • Glycoproteins
  • Multiprotein Complexes
  • Viral Envelope Proteins