EspA, a protein secreted by enteropathogenic Escherichia coli, is required to induce signals in epithelial cells.

Abstract:

:Enteropathogenic Escherichia coli (EPEC) is a leading cause of infant diarrhoea. EPEC mediates several effects on host epithelial cells, including activation of signal-transduction pathways, cytoskeletal rearrangement along with pedestal and attaching/effacing lesion formation. It has been previously shown that the EPEC eaeB (espB) gene encodes a secreted protein required for signal transduction and adherence, while eaeA encodes intimin, an EPEC membrane protein that mediates intimate adherence and contributes to focusing of cytoskeletal proteins beneath bacteria. DNA-sequence analysis of a region between eaeA and eaeB identified a predicted open reading frame (espA) that matched the amino-terminal sequence of a 25 kDa EPEC secreted protein. A mutant with a non-polar insertion in espA does not secrete this protein, activate epithelial cell signal transduction or cause cytoskeletal rearrangement. These phenotypes were complemented by a cloned espA gene. The espA mutant is also defective for invasion. It is concluded that espA encodes an EPEC secreted protein that is necessary for activating epithelial signal transduction, intimate contact, and formation of attaching and effacing lesions, processes which are central to pathogenesis.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Kenny B,Lai LC,Finlay BB,Donnenberg MS

doi

10.1111/j.1365-2958.1996.tb02619.x

subject

Has Abstract

pub_date

1996-04-01 00:00:00

pages

313-23

issue

2

eissn

0950-382X

issn

1365-2958

journal_volume

20

pub_type

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