Dec 9, 1997

Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells

Cell
Brendan KennyB B Finlay

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.

Mentioned in this Paper

Actin Nucleation
Bacterial Proteins
Alkalescens-Dispar Group
Pathogenicity
Chimeric Proteins, Recombinant
Tir protein, E coli
Pathogenic Organism
Hormone Receptors, Cell Surface
Actins
Outer Membrane Lipoproteins, Bacterial

About this Paper

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