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The intimin–translocated intimin receptor (Tir) interaction is a key molecular event enabling the attachment of certain pathogenic *Escherichia coli* (notably enteropathogenic and enterohemorrhagic strains, EPEC and EHEC) to the surface of **intestinal epithelial cells**[1][3][5][9]. Shortly after infection, these bacteria use a type III secretion system to inject Tir into host cell membranes, where Tir functions as a receptor for the bacterial surface adhesin intimin. This high-affinity interaction is essential for the formation of attaching and effacing lesions, leading to the localized destruction of intestinal microvilli and rearrangement of the host actin cytoskeleton to form pedestal-like structures beneath the adherent bacteria[1][3][5][7][9]. The intimin–Tir engagement also manipulates host cell signaling and immune responses, supporting successful colonization and persistence in the intestine. This interaction is central to the virulence of A/E pathogens and represents a potential therapeutic target, although so far, no drugs have reached clinical application that inhibit this specific interaction.
Potential therapeutics would block intimin–Tir binding to inhibit bacterial colonization and lesion formation
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