title: Tir tyrosine phosphorylation and pedestal formation are delayed in enteropathogenic Escherichia coli sepZ::TnphoA mutant 30-5-1(3).
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.
authors: Biotechnology Laboratory, University of British Columbia, Vancouver, British Columbia, V6T 1Z3, Canada.
authors: R
authors: R
authors: Devinney
authors: I
authors: I
authors: Nisan
authors: S
authors: S
authors: Ruschkowski
authors: I
authors: I
authors: Rosenshine
authors: B B
authors: BB
authors: Finlay
mesh_terms: D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000032:analysis / Q000235:genetics* / Q000502:physiology; D004251:DNA Transposable Elements; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity*; D029968:Escherichia coli Proteins; D006367:HeLa Cells; D006801:Humans; D009154:Mutation; D010766:Phosphorylation; D011956:Receptors, Cell Surface / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D004251:DNA Transposable Elements; D029968:Escherichia coli Proteins; C102051:EspA protein, E coli; D011956:Receptors, Cell Surface; C103307:SepZ protein, E coli; C109287:Tir protein, E coli; D014443:Tyrosine