Induction of secretion of interleukin-8 from human gastric epithelial cells by heat-shock protein 60 homologue of Helicobacter pylori

J Med Microbiol. 1999 Oct;48(10):927-933. doi: 10.1099/00222615-48-10-927.

Abstract

Escherichia coli cells expressing fusion proteins consisting of beta-galactosidase and bacterial heat-shock protein (HSP) 60 of E. coli, Yersinia enterocolitica or Helicobacter pylori were constructed, and designated as HY1, HY2 or HY3, respectively. Fusion proteins prepared from HY2 and HY3 induced secretion of interleukin-8 (IL-8) from human gastric epithelial KATOIII cell cultures. On the other hand, the parent strain (E. coli pop2136), PEX (pop2136 transformed by vector) and fusion protein prepared from HY1 did not induce IL-8 secretion from KATOIII cells. Other human gastric (MKN45) and non-gastric cell lines (Int 407 and A549) did not secrete IL-8 following treatment with these proteins. These results indicate that H. pylori HSP60 induces IL-8 secretion from human gastric cells and the levels of IL-8 differ among the various gastric cell lines, suggesting that HSP60 might be an important virulence factor associated with chronic gastric inflammation following H. pylori infection in man.

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / pharmacology*
  • Cell Line
  • Dose-Response Relationship, Drug
  • Electrophoresis, Polyacrylamide Gel
  • Epithelial Cells / drug effects
  • Epithelial Cells / metabolism
  • Gastric Mucosa / drug effects*
  • Gastric Mucosa / metabolism
  • Helicobacter pylori / metabolism
  • Helicobacter pylori / pathogenicity*
  • Humans
  • Immunoblotting
  • Interleukin-8 / metabolism*
  • Molecular Sequence Data
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / pharmacology
  • Transfection
  • Virulence

Substances

  • 60K protein, Helicobacter pylori
  • Bacterial Proteins
  • Interleukin-8
  • Recombinant Fusion Proteins