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RNA Interference-based Investigation of the Function of Heat Shock Protein 27 during Corneal Epithelial Wound Healing
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RNA Interference-based Investigation of the Function of Heat Shock Protein 27 during Corneal Epithelial Wound Healing

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Heat shock protein 27 mediated signaling in viral infection

Jaya Rajaiya1, Mohammad A Yousuf, Gurdeep Singh

  • 1Howe Laboratory, Mass Eye and Ear Infirmary, Department of Ophthalmology, Harvard Medical School, Boston, MA 02114, USA.

Biochemistry
|June 28, 2012
PubMed

Insights

Heat shock protein 27 (HSP27) forms a complex with p38 and NFκB-p65 in virus-infected cells. This novel HSP27-mediated association is crucial for inflammatory gene expression.

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Immunology

Background:

  • Heat shock proteins (HSPs), particularly small HSPs, are involved in cellular functions like IL-8 induction.
  • Human adenovirus infection triggers intracellular signaling pathways, including those involving c-Src and mitogen-activated protein kinases (MAPKs).
  • p38 MAPK signaling is known to mediate the expression of inflammatory mediators like IL-8 and MCP-1, involving NFκB-p65 activation.

Purpose of the Study:

  • To investigate the novel role of heat shock protein 27 (HSP27) in the interaction between p38 and NFκB-p65 during viral infection.
  • To elucidate the mechanism by which HSP27 influences the formation of signaling complexes and downstream inflammatory gene expression.

Main Methods:

  • Immunoprecipitation assays were used to detect protein-protein interactions in virus-infected cells.
  • Short interfering RNA (siRNA) targeting HSP27 was employed to assess its role in signaling complex formation and gene expression.
  • Transfection with tagged p38 mutants identified specific amino acid residues critical for p38-NFκB-p65 association.

Main Results:

  • A signaling complex comprising p38 and NFκB-p65 was identified in virus-infected cells.
  • Disruption of HSP27 using siRNA abrogated the p38-NFκB-p65 association and reduced IL-8 expression.
  • HSP27 siRNA also decreased the nuclear translocation of both NFκB-p65 and p38.
  • Amino acids 279-347 of p38 were found to be essential for its association with NFκB-p65.

Conclusions:

  • HSP27, p38, and NFκB-p65 form a functional signalosome in virus-infected cells.
  • This HSP27-dependent signalosome complex regulates the expression of pro-inflammatory mediators.
  • HSP27 plays a critical role in mediating inflammatory responses during viral infections.

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