| Helicobacter pylori-induced homotypic phagosome fusion in human monocytes is independent of the bacterial vacA and cag status. | |
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MedLine Citation:
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PMID: 14641174 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Following reports that a VacA+cag+ toxigenic but not a VacA-cag- non-toxigenic Helicobacter pylori strain induced homotypic phagosome fusion in murine macrophages, we addressed that phenomenon in human cells. Mononuclear phagocytes and epitheloid cells were challenged with H. pylori strains of different vacA and cag genotypes and with VacA- and Cag- isogenic mutants, and chased in the absence or presence of signal transduction modulators. Electron microscopy revealed that, in monocytes: (i) homotypic phagosome fusion was frequently induced by all live H. pylori strains investigated but not by exogenous VacA; (ii) phagosomes containing bacteria fused, but not those containing latex beads; (iii) fusion resulted in communal compartments resembling giant multivesicular bodies; and (iv) formation of these compartments was blocked by inhibiting the host cell regulators PI 3-kinase, phospholipase C and p42 MAP kinase. Whereas some internalized bacteria remained viable 1 h after uptake, none survived a 24 h period. In contrast to monocytes, infected epitheloid cells rarely developed communal compartments. In combination, these results demonstrate that, in human monocytes, the H. pylori-induced homotypic phagosome fusion depends on neither the vacuolating cytotoxin VacA nor the cag pathogenicity island of H. pylori and does not result in prolonged intracellular survival. |
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Authors:
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M G Rittig; B Shaw; D P Letley; R J Thomas; R H Argent; J C Atherton |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Cellular microbiology Volume: 5 ISSN: 1462-5814 ISO Abbreviation: Cell. Microbiol. Publication Date: 2003 Dec |
Date Detail:
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Created Date: 2003-12-03 Completed Date: 2004-03-09 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 100883691 Medline TA: Cell Microbiol Country: England |
Other Details:
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Languages: eng Pagination: 887-99 Citation Subset: IM |
Affiliation:
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Centre for Biochemistry and Cell Biology, Institute of Infections, Immunity and Inflammation, University of Nottingham Meeical School, UK. michael.rittig@nottingham.ac.uk |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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1-Phosphatidylinositol 3-Kinase
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antagonists & inhibitors Androstadienes / pharmacology Bacterial Proteins / genetics, metabolism Cell Line Chromones / pharmacology Colony Count, Microbial Epithelioid Cells / microbiology*, ultrastructure Estrenes / pharmacology Gene Deletion Genes, Bacterial / genetics Helicobacter pylori / genetics, pathogenicity* Humans Microscopy, Electron Microspheres Mitogen-Activated Protein Kinase 1 / antagonists & inhibitors Monocytes / microbiology*, ultrastructure Morpholines / pharmacology Mutagenesis, Insertional Phagosomes / microbiology*, physiology, ultrastructure Pyrrolidinones / pharmacology Type C Phospholipases / antagonists & inhibitors Tyrphostins / pharmacology |
| Chemical | |
Reg. No./Substance:
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0/Androstadienes; 0/Bacterial Proteins; 0/Chromones; 0/Estrenes; 0/Morpholines; 0/PicB protein, Helicobacter pylori; 0/Pyrrolidinones; 0/Tyrphostins; 0/VacA protein, Helicobacter pylori; 112648-68-7/1-(6-((3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dione; 118409-62-4/AG 127; 154447-36-6/2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one; 19545-26-7/wortmannin; EC 2.7.1.137/1-Phosphatidylinositol 3-Kinase; EC 2.7.11.24/Mitogen-Activated Protein Kinase 1; EC 3.1.4.-/Type C Phospholipases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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