Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion

EMBO Rep. 2010 Oct;11(10):798-804. doi: 10.1038/embor.2010.114. Epub 2010 Sep 3.

Abstract

Mammalian and prokaryotic high-temperature requirement A (HtrA) proteins are chaperones and serine proteases with important roles in protein quality control. Here, we describe an entirely new function of HtrA and identify it as a new secreted virulence factor from Helicobacter pylori, which cleaves the ectodomain of the cell-adhesion protein E-cadherin. E-cadherin shedding disrupts epithelial barrier functions allowing H. pylori designed to access the intercellular space. We then designed a small-molecule inhibitor that efficiently blocks HtrA activity, E-cadherin cleavage and intercellular entry of H. pylori.

MeSH terms

  • Bacterial Adhesion
  • Bacterial Outer Membrane Proteins / metabolism*
  • Blotting, Western
  • Cadherins / metabolism*
  • Cell Adhesion Molecules / metabolism
  • Cell Line, Tumor
  • Epithelial Cells / metabolism
  • Helicobacter Infections / metabolism
  • Helicobacter pylori / genetics*
  • Helicobacter pylori / metabolism*
  • Humans
  • Virulence Factors / metabolism*

Substances

  • Bacterial Outer Membrane Proteins
  • Cadherins
  • Cell Adhesion Molecules
  • Virulence Factors