Localization of heat shock proteins in clinical Actinobacillus actinomycetemcomitans strains and their effects on epithelial cell proliferation

FEMS Microbiol Lett. 2000 Jan 15;182(2):231-5. doi: 10.1111/j.1574-6968.2000.tb08900.x.

Abstract

Actinobacillus actinomycetemcomitans is an important pathogen in periodontitis. In the present study we localized the GroEL- and DnaK-like heat shock proteins (Hsp) in subcellular fractions of 12 A. actinomycetemcomitans strains of various clinical origin and compared their effects on periodontal epithelial cell proliferation and viability. In all strains, GroEL-like protein was found in the membrane, cytoplasm, and periplasm, whereas DnaK-like protein was present in the cytoplasm and periplasm. No correlation was observed between the Hsp expression and the serotype or origin of A. actinomycetemcomitans strains. The bacterial membrane fractions that expressed the GroEL-like protein moderately or strongly induced epithelial cell proliferation more strongly than strains that expressed the protein weakly. The results suggest that GroEL-like Hsp may play a role in the virulence of A. actinomycetemcomitans by increasing epithelial proliferation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actinobacillus Infections / microbiology*
  • Adolescent
  • Adult
  • Aged
  • Aggregatibacter actinomycetemcomitans / chemistry*
  • Animals
  • Cell Division
  • Cell Membrane / chemistry
  • Cells, Cultured
  • Chaperonin 60 / analysis*
  • Chaperonin 60 / physiology
  • Child
  • Cytoplasm / chemistry
  • Electrophoresis, Polyacrylamide Gel
  • Epithelial Cells / cytology*
  • Escherichia coli Proteins*
  • Female
  • HSP70 Heat-Shock Proteins / analysis*
  • HSP70 Heat-Shock Proteins / physiology
  • Humans
  • Immunoblotting
  • Male
  • Middle Aged
  • Periodontal Ligament / cytology
  • Periodontitis / microbiology
  • Swine

Substances

  • Chaperonin 60
  • Escherichia coli Proteins
  • HSP70 Heat-Shock Proteins
  • dnaK protein, E coli