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.
journal_name
Celljournal_title
Cellauthors
Kenny B,DeVinney R,Stein M,Reinscheid DJ,Frey EA,Finlay BBdoi
10.1016/s0092-8674(00)80437-7subject
Has Abstractpub_date
1997-11-14 00:00:00pages
511-20issue
4eissn
0092-8674issn
1097-4172pii
S0092-8674(00)80437-7journal_volume
91pub_type
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