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Abstract
Enteropathogenic E. coli (EPEC) belongs to a group of bacterial pathogens that induce
epithelial cell actin rearrangements resulting in pedestal formation beneath adherent
bacteria. This requires the secretion of specific virulence proteins needed for signal
transduction and intimate adherence. EPEC interaction induces tyrosine phosphorylation
of a protein in the host membrane, Hp90, which is the receptor for the EPEC outer
membrane protein, intimin. Hp90-intimin interaction is essential for intimate attachment
and pedestal formation. Here, we demonstrate that Hp90 is actually a bacterial protein
(Tir). Thus, this bacterial pathogen inserts its own receptor into mammalian cell
surfaces, to which it then adheres to trigger additional host signaling events and
actin nucleation. It is also tyrosine-phosphorylated upon transfer into the host cell.