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Intimate bacterial adhesion to intestinal epithelium is a pathogenic mechanism shared by several human and animal enteric pathogens, including enteropathogenic and enterohaemorrhagic Escherichia coli and Citrobacter rodentium. The proteins directly involved in this process are the outer-membrane adhesion molecule intimin and the translocated intimin receptor, Tir. The receptor-binding activity of intimin resides within the carboxy terminus 280 aa (Int280) of the polypeptide. Four tryptophan residues, W117/776, W136/795, W222/881 and W240/899, are conserved within different Int280 molecules that otherwise show considerable sequence variation. In this study the influence of site-directed mutagenesis of each of the four tryptophan residues on intimin-Tir interactions and on intimin-mediated intimate attachment was determined. The mutant intimins were also studied using a variety of in vitro and in vivo infection models. The results show that all the substitutions modulated intimin activity, although some mutations had more profound effects than others.

Original publication




Journal article



Publication Date





657 - 665


Adhesins, Bacterial, Amino Acid Sequence, Animals, Bacterial Adhesion, Carrier Proteins, Cell Line, Citrobacter freundii, Colon, Disease Models, Animal, Enterobacteriaceae Infections, Escherichia coli Proteins, Female, Humans, Mice, Mice, Inbred C3H, Molecular Sequence Data, Mutagenesis, Site-Directed, Receptors, Cell Surface, Tryptophan, Virulence