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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1997-12-23
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adhesins, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/EaeB protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/EspA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/eaeA protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
511-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9390560-Adhesins, Bacterial,
pubmed-meshheading:9390560-Amino Acid Sequence,
pubmed-meshheading:9390560-Antibodies, Bacterial,
pubmed-meshheading:9390560-Bacterial Adhesion,
pubmed-meshheading:9390560-Bacterial Outer Membrane Proteins,
pubmed-meshheading:9390560-Bacterial Proteins,
pubmed-meshheading:9390560-Base Sequence,
pubmed-meshheading:9390560-Carrier Proteins,
pubmed-meshheading:9390560-Cell Membrane,
pubmed-meshheading:9390560-Escherichia coli,
pubmed-meshheading:9390560-Escherichia coli Proteins,
pubmed-meshheading:9390560-Genes, Bacterial,
pubmed-meshheading:9390560-HeLa Cells,
pubmed-meshheading:9390560-Humans,
pubmed-meshheading:9390560-Isoelectric Point,
pubmed-meshheading:9390560-Molecular Sequence Data,
pubmed-meshheading:9390560-Molecular Weight,
pubmed-meshheading:9390560-Mutation,
pubmed-meshheading:9390560-Phosphorylation,
pubmed-meshheading:9390560-Receptors, Cell Surface,
pubmed-meshheading:9390560-Recombinant Fusion Proteins,
pubmed-meshheading:9390560-Restriction Mapping,
pubmed-meshheading:9390560-Tyrosine,
pubmed-meshheading:9390560-Virulence
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pubmed:year |
1997
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pubmed:articleTitle |
Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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