Enteropathogenic E. coli (EPEC) Transfers Its Receptor for Intimate Adherence into Mammalian Cells

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...

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Bibliographic Details
Published in:Cell 1997-11, Vol.91 (4), p.511-520
Main Authors: Kenny, Brendan, DeVinney, Rebekah, Stein, Markus, Reinscheid, Dieter J, Frey, Elizabeth A, Finlay, B.Brett
Format: Article
Language:English
Subjects:
Adhesins, Bacterial
Amino Acid Sequence
Antibodies, Bacterial
Bacterial Adhesion - genetics
Bacterial Outer Membrane Proteins - genetics
Bacterial Outer Membrane Proteins - metabolism
Bacterial Outer Membrane Proteins - physiology
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - isolation & purification
Bacterial Proteins - metabolism
Bacterial Proteins - physiology
Base Sequence
Carrier Proteins
Cell Membrane - chemistry
Cell Membrane - metabolism
Escherichia coli - genetics
Escherichia coli - immunology
Escherichia coli - pathogenicity
Escherichia coli Proteins
Genes, Bacterial - genetics
HeLa Cells
Humans
Isoelectric Point
Molecular Sequence Data
Molecular Weight
Mutation
Phosphorylation
Receptors, Cell Surface - chemistry
Receptors, Cell Surface - genetics
Receptors, Cell Surface - isolation & purification
Receptors, Cell Surface - metabolism
Recombinant Fusion Proteins - analysis
Restriction Mapping
Tyrosine - metabolism
Virulence
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Summary: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.
ISSN:0092-8674
1097-4172
DOI:10.1016/S0092-8674(00)80437-7