Linked Life Data

12864848

Source:http://linkedlifedata.com/resource/pubmed/id/12864848

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pubmed-article:12864848pubmed:abstractTextGonorrhea 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.lld:pubmed
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pubmed-article:12864848pubmed:dateRevised2011-11-17lld:pubmed
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pubmed-article:12864848pubmed:articleTitleImmunoreceptor tyrosine-based activation motif phosphorylation during engulfment of Neisseria gonorrhoeae by the neutrophil-restricted CEACAM3 (CD66d) receptor.lld:pubmed
pubmed-article:12864848pubmed:affiliationDepartment of Medical Genetics and Microbiology, University of Toronto, Toronto, Canada.lld:pubmed
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pubmed-article:12864848pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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