Chaperone fusion proteins aid entropy-driven maturation of class II viral fusion proteins

Trends Microbiol. 2014 Feb;22(2):100-6. doi: 10.1016/j.tim.2013.11.006. Epub 2013 Dec 28.

Abstract

Class II viral fusion proteins are present on the envelope of flaviviruses and togaviruses, viruses that often cause tropical and subtropical diseases. These proteins use a second membrane protein as a molecular chaperone to assist their folding and to ensure proper function during viral assembly, maturation, and infection. Recent progress in structural studies of dengue viruses has revealed how the chaperone pre-membrane (prM) protein guides viral maturation and how pH is sensed in both the maturation and infection processes. Drastic conformation changes and reorganization of these viral membrane proteins occur during the transition from their metastable to stable structural states in a unidirectional, entropy-driven process.

Keywords: bio-threat agent; cryo-electron microscopy; enveloped viruses; flavivirus; structures; togavirus.

Publication types

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

MeSH terms

  • Dengue Virus / drug effects
  • Dengue Virus / enzymology*
  • Entropy*
  • Hydrogen-Ion Concentration
  • Molecular Chaperones / metabolism*
  • Protein Conformation
  • Protein Folding*
  • Viral Envelope Proteins / metabolism*
  • Viral Fusion Proteins / metabolism*

Substances

  • Molecular Chaperones
  • Viral Envelope Proteins
  • Viral Fusion Proteins
  • prM protein, Flavivirus