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Intimin is a 94 kDa outer membrane protein and a critical virulence factor found in Enteropathogenic Escherichia coli (EPEC) and Enterohemorrhagic E. coli (EHEC) [2, 3]. It is encoded by the eae gene and functions as an adhesin that mediates the intimate attachment of bacteria to host intestinal epithelial cells [1, 5]. This attachment is achieved through a unique mechanism where the bacteria first inject their own receptor, the Translocated intimin receptor (Tir), into the host cell membrane via a Type III secretion system [2, 7]. Intimin then binds to the extracellular domain of Tir, triggering a signaling cascade that leads to actin polymerization and the formation of characteristic pedestal structures, known as attaching and effacing (A/E) lesions [5, 11]. Because intimin is essential for colonization and pathogenesis, it is a primary target for the development of anti-adhesion therapies and vaccines aimed at preventing EHEC and EPEC infections [4, 10]. Current therapeutic strategies focus on using recombinant intimin fragments or anti-intimin antibodies to block bacterial binding, thereby neutralizing the pathogen's ability to cause disease without exerting the selective pressure associated with traditional antibiotics [9, 16].
Inhibition of bacterial adhesion to host intestinal epithelial cells by blocking the Intimin-Tir interaction.
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