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Article

Insertion of the enteropathogenic Escherichia coli Tir virulence protein into membranes in vitro.

The Journal of biological chemistry - 24 Mar 2006

Race Paul R, Lakey Jeremy H, Banfield Mark J

Abstract excerpt

Insertion of the enteropathogenic Escherichia coli Tir protein into the plasma membrane of intestinal epithelial cells is a crucial event in infection because it provides a receptor for intimate bacterial adherence. This interaction with the bacterial outer membrane protein intimin is also essential in generating a number of signaling activities associated with virulence. Tir can be modified at various sites by...

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Identifiers

PMID: 16436373
DOI: 10.1074/jbc.M513532200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Insertion of the enteropathogenic Escherichia coli Tir virulence protein into membranes in vitro.PMID 16436373Read ↗

Identification of the intimin-binding domain of Tir of enteropathogenic Escherichia coli.Semantic proximity Read ↗

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Mechanical fractionation reveals structural requirements for enteropathogenic Escherichia coli Tir insertion into host membranes.Semantic proximity Read ↗

A carboxy-terminal domain of Tir from enterohemorrhagic Escherichia coli O157:H7 (EHEC O157:H7) required for efficient type III secretion.Semantic proximity Read ↗

The enterohaemorrhagic Escherichia coli (serotype O157:H7) Tir molecule is not functionally interchangeable for its enteropathogenic E. coli (serotype O127:H6) homologueSemantic proximity Read ↗

Enteropathogenic Escherichia coli translocated intimin receptor, Tir, requires a specific chaperone for stable secretion.Semantic proximity Read ↗

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