Evidence for an association between heat shock protein 70 and the respiratory syncytial virus polymerase complex within lipid-raft membranes during virus infection

Virology. 2005 Jul 20;338(1):69-80. doi: 10.1016/j.virol.2005.05.004.

Abstract

In this report, the interaction between respiratory syncytial virus (RSV) and heat shock protein 70 (HSP70) was examined. Although no significant increase in total HSP70 protein levels was observed during virus infection, analysis of the HSP70 content in lipid-raft membranes from mock- and virus-infected cells revealed an increase in the levels of raft-associated HSP70 during virus infection. Fluorescence microscopy demonstrated that this transport of HSP70 into lipid-raft membranes correlated with the appearance of HSP70 within virus-induced inclusion bodies. Furthermore, co-localisation of HSP70 with the virus N protein and the raft lipid GM1 was observed within these structures. Immunoprecipitation experiments demonstrated the ability of HSP70 to interact with the virus polymerase complex in lipid-rafts in an ATP-dependent manner. Collectively, these data suggest that RSV may induce cellular changes which allow the recruitment of specific host-cell factors, via lipid-raft membranes, to the polymerase complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Line
  • HSP70 Heat-Shock Proteins / genetics
  • HSP70 Heat-Shock Proteins / physiology*
  • Humans
  • Inclusion Bodies / physiology
  • Inclusion Bodies / virology
  • Membrane Microdomains / physiology*
  • Membrane Microdomains / virology*
  • Microscopy, Fluorescence
  • Molecular Sequence Data
  • Multiprotein Complexes
  • Peptide Fragments / genetics
  • Peptide Fragments / isolation & purification
  • Respiratory Syncytial Viruses / genetics
  • Respiratory Syncytial Viruses / pathogenicity*
  • Respiratory Syncytial Viruses / physiology*
  • Viral Proteins / genetics
  • Viral Proteins / physiology*
  • Virus Replication

Substances

  • HSP70 Heat-Shock Proteins
  • Multiprotein Complexes
  • Peptide Fragments
  • Viral Proteins