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Characterization of a cDNA clone, encoding a 70 kDa heat shock protein from the dermatophyte pathogen Trichophyton

S Rezaie1, J Ban, M Mildner

  • 1Division of Immunology, Allergy and Infectious Diseases, Department of Dermatology, University of Vienna Medical School, Währinger Gürtel 18-20, A-1090, Vienna, Austria.

Gene
|December 23, 1999
PubMed

Insights

Researchers cloned and characterized the first 70kDa heat-shock protein (HSP) from Trichophyton rubrum, a common cause of chronic fungal infections. This HSP is constitutively expressed and up-regulated by heat stress.

Area of Science:

  • Medical Mycology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Trichophyton rubrum causes most chronic dermatophytosis.
  • Understanding pathogen proteins is crucial for molecular characterization.
  • Heat-shock proteins (HSPs) are vital cellular components.

Purpose of the Study:

  • To clone and characterize the 70kDa heat-shock protein (HSP70) gene from Trichophyton rubrum.
  • To analyze the expression patterns of the identified HSP70 gene.
  • To determine the HSP70 gene family size in T. rubrum.

Main Methods:

  • cDNA library construction from T. rubrum.
  • Recombinant protein expression and detection via Western blot.
  • Genomic DNA analysis using Southern blot.
  • RNA expression analysis via Northern blot.

Main Results:

  • A recombinant cDNA clone identical to eukaryotic 70kDa heat-shock proteins (HSPs) was identified.
  • Southern blot analysis indicated a single HSP70 gene family member in T. rubrum.
  • The HSP70 gene contains two introns.
  • Northern blot revealed constitutive expression at 27°C, with strong upregulation at 37°C.

Conclusions:

  • The first HSP gene from a dermatophyte, T. rubrum, was cloned and identified as a member of the DnaK subfamily of 70kDa HSPs.
  • The characterized HSP70 exhibits heat-inducible expression, suggesting a role in stress response.
  • This study provides a molecular basis for further investigation into T. rubrum pathogenesis and stress adaptation.

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