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Heat-shock protein 70 and heat-shock protein 90 associate with Toll-like receptor 4 in response to bacterial

M Triantafilou1, K Triantafilou

  • 1Infection and Immunity Group, University of Sussex, School of Life Sciences, Falmer, Brighton, BN1 9QG, UK.

Biochemical Society Transactions
|July 24, 2004
PubMed

Insights

Heat-shock proteins (Hsps) associate with Toll-like receptor 4 (TLR4) upon bacterial lipopolysaccharide (LPS) stimulation. These Hsps are involved in TLR4 trafficking to the Golgi, shedding light on innate immune responses.

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Mammalian cells recognize bacterial lipopolysaccharide (LPS) via receptors like Toll-like receptor 4 (TLR4).
  • Heat-shock proteins (Hsps) have been implicated in innate immune recognition of bacterial products.
  • The precise role and cell surface presence of Hsps in LPS recognition remain unclear.

Purpose of the Study:

  • To investigate the association between heat-shock proteins (Hsp70 and Hsp90) and Toll-like receptor 4 (TLR4) after LPS stimulation.
  • To determine the cellular localization (cell surface and intracellular) of this Hsp-TLR4 interaction.
  • To elucidate the role of Hsps in the trafficking of TLR4 in response to LPS.

Main Methods:

  • Stimulation of cells with bacterial lipopolysaccharide (LPS).
  • Immunoprecipitation and Western blotting to detect protein-protein interactions (TLR4, Hsp70, Hsp90).
  • Cell surface and intracellular protein localization studies, including co-localization with Golgi markers.

Main Results:

  • Hsp70 and Hsp90 form clusters with TLR4 within lipid microdomains following LPS stimulation.
  • Both Hsp70 and Hsp90 are co-targeted to the Golgi apparatus along with TLR4 upon LPS stimulation.
  • This suggests a role for Hsps in the intracellular trafficking of the TLR4/LPS complex.

Conclusions:

  • Heat-shock proteins (Hsp70, Hsp90) are integral components of the TLR4 signaling complex during LPS recognition.
  • Hsps play a role in the cellular trafficking of TLR4, particularly its transport to the Golgi apparatus.
  • These findings expand our understanding of the mechanisms underlying innate immune responses to bacterial components.

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