The CGM1a (CEACAM3/CD66d)-mediated Phagocytic Pathway of Neisseria gonorrhoeae Expressing Opacity Proteins Is Also the Pathway to Cell Death
| Autor: | Wolfgang Zimmermann, Fritz Grunert, Milica Pantelic, Ines Chen, Silvia Bolland, James Parker, Tie Chen |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Programmed cell death
Neutrophils Phagocytosis Molecular Sequence Data Syk In Vitro Techniques Biology Transfection Biochemistry Cell Line Cell membrane Calcium flux medicine Animals Humans Syk Kinase Amino Acid Sequence Tyrosine Molecular Biology Antigens Bacterial B-Lymphocytes Enzyme Precursors Cell Death Cell Membrane Intracellular Signaling Peptides and Proteins Cell Biology Protein-Tyrosine Kinases Neisseria gonorrhoeae Recombinant Proteins Carcinoembryonic Antigen Cell biology medicine.anatomical_structure Calcium Signal transduction Cell Adhesion Molecules Chickens Bacterial Outer Membrane Proteins |
| Zdroj: | Journal of Biological Chemistry. 276:17413-17419 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m010609200 |
| Popis: | Phagocytosis of Opa+ Neisseria gonorrhoeae (gonococcus, GC) by neutrophils is in part dependent on the interaction of Opa proteins with CGM1a (CEACAM3/CD66d) antigens, a neutrophil-specific receptor. However, the signaling pathways leading to phagocytosis have not been characterized. Here we show that interaction of OpaI bacteria with neutrophils or CGM1a-transfected DT40 cells induces calcium flux, which correlates with phagocytosis of bacteria. We identified an immunoreceptor tyrosine-based activation motif (ITAM) in CGM1a, and showed that the ability of CGM1a to transduce signals and mediate phagocytosis was abolished by mutation of the ITAM tyrosines. We also demonstrated that CGM1a-ITAM-mediated bacterial phagocytosis is dependent on Syk and phospholipase C activity in DT40 cells. Unexpectedly, the activation of the CGM1a-ITAM phagocytic pathway by Opa+ GC results in induction of cell death. |
| Databáze: | OpenAIRE |
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