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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2003-7-16
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pubmed:abstractText |
Gonorrhea is characterized by a purulent urethral or cervical discharge consisting primarily of neutrophils associated with Neisseria gonorrhoeae. These interactions are facilitated by gonococcal colony opacity-associated (Opa) protein binding to host cellular CEACAM receptors. Of these, CEACAM3 is restricted to neutrophils and contains an immunoreceptor tyrosine-based activation motif (ITAM) reminiscent of that found within certain phagocytic Fc receptors. CEACAM3 was tyrosine phosphorylated by a Src family kinase-dependent process upon infection by gonococci expressing CEACAM-specific Opa proteins. This phosphorylation was necessary for efficient bacterial uptake; however, a less efficient uptake process became evident when kinase inhibitors or mutagenesis of the ITAM were used to prevent phosphorylation. Ligated CEACAM3 was recruited to a cytoskeleton-containing fraction, intense foci of polymerized actin were evident where bacteria attached to HeLa-CEACAM3, and disruption of polymerized actin by cytochalasin D blocked all bacterial uptake by these cells. These data support a model whereby CEACAM3 can mediate the Opa-dependent uptake of N. gonorrhoeae via either an efficient, ITAM phosphorylation-dependent process that resembles phagocytosis or a less efficient, tyrosine phosphorylation-independent mechanism.
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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/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CEACAM3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carcinoembryonic Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/opacity factor receptor, Neisseria...,
http://linkedlifedata.com/resource/pubmed/chemical/opacity proteins,
http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0950-382X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
49
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
623-37
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:12864848-Actin Cytoskeleton,
pubmed-meshheading:12864848-Adhesins, Bacterial,
pubmed-meshheading:12864848-Amino Acid Motifs,
pubmed-meshheading:12864848-Amino Acid Sequence,
pubmed-meshheading:12864848-Antigens, Bacterial,
pubmed-meshheading:12864848-Bacterial Proteins,
pubmed-meshheading:12864848-Carcinoembryonic Antigen,
pubmed-meshheading:12864848-Cytoskeleton,
pubmed-meshheading:12864848-HeLa Cells,
pubmed-meshheading:12864848-Humans,
pubmed-meshheading:12864848-Molecular Sequence Data,
pubmed-meshheading:12864848-Neisseria gonorrhoeae,
pubmed-meshheading:12864848-Neutrophils,
pubmed-meshheading:12864848-Phosphorylation,
pubmed-meshheading:12864848-Protein Processing, Post-Translational,
pubmed-meshheading:12864848-Proteoglycans,
pubmed-meshheading:12864848-Receptors, Cell Surface,
pubmed-meshheading:12864848-Recombinant Fusion Proteins,
pubmed-meshheading:12864848-Transfection,
pubmed-meshheading:12864848-src-Family Kinases
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pubmed:year |
2003
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pubmed:articleTitle |
Immunoreceptor tyrosine-based activation motif phosphorylation during engulfment of Neisseria gonorrhoeae by the neutrophil-restricted CEACAM3 (CD66d) receptor.
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pubmed:affiliation |
Department of Medical Genetics and Microbiology, University of Toronto, Toronto, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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