Tir tyrosine phosphorylation and pedestal formation are delayed in enteropathogenic Escherichia coli sepZ::TnphoA mutant 30-5-1(3)

Infect Immun. 2001 Jan;69(1):559-63. doi: 10.1128/IAI.69.1.559-563.2001.

Abstract

Enteropathogenic Escherichia coli (EPEC) strain 30-5-1(3) has been reported to form attaching and effacing (A/E) lesions without Tir tyrosine phosphorylation. In this study, we show that 30-5-1(3), which has a transposon insertion within the sepZ gene, forms wild-type A/E lesions including Tir tyrosine phosphorylation, but at a slower rate. A/E lesion formation by 30-5-1(3) occurs without detectable secretion of Tir or other EPEC Esp secreted proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Adhesion
  • Bacterial Proteins / analysis
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / physiology
  • DNA Transposable Elements*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli / pathogenicity*
  • Escherichia coli Proteins*
  • HeLa Cells
  • Humans
  • Mutation
  • Phosphorylation
  • Receptors, Cell Surface / metabolism*
  • Tyrosine / metabolism*

Substances

  • Bacterial Proteins
  • DNA Transposable Elements
  • Escherichia coli Proteins
  • EspA protein, E coli
  • Receptors, Cell Surface
  • SepZ protein, E coli
  • Tir protein, E coli
  • Tyrosine