Modes of paramyxovirus fusion: a Henipavirus perspective

Trends Microbiol. 2011 Aug;19(8):389-99. doi: 10.1016/j.tim.2011.03.005. Epub 2011 Apr 20.

Abstract

Henipavirus is a new genus of Paramyxoviridae that uses protein-based receptors (ephrinB2 and ephrinB3) for virus entry. Paramyxovirus entry requires the coordinated action of the fusion (F) and attachment viral envelope glycoproteins. Receptor binding to the attachment protein triggers F to undergo a conformational cascade that results in membrane fusion. The accumulation of structural and functional studies on many paramyxoviral fusion and attachment proteins, including the recent elucidation of structures of Nipah virus (NiV) and Hendra virus (HeV) G glycoproteins bound and unbound to cognate ephrinB receptors, indicate that henipavirus entry and fusion could differ mechanistically from paramyxoviruses that use glycan-based receptors.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Glycosylation
  • Henipavirus / metabolism
  • Henipavirus / physiology*
  • Host-Pathogen Interactions
  • Humans
  • Membrane Fusion*
  • Phylogeny
  • Protein Conformation
  • Receptors, Cell Surface / metabolism
  • Receptors, Cell Surface / physiology
  • Receptors, Eph Family / metabolism
  • Receptors, Virus / metabolism
  • Receptors, Virus / physiology
  • Viral Envelope Proteins / metabolism*
  • Virus Attachment*
  • Virus Internalization

Substances

  • F protein, Nipah virus
  • Receptors, Cell Surface
  • Receptors, Virus
  • Viral Envelope Proteins
  • attachment protein G
  • sialic acid receptor
  • Receptors, Eph Family