| pubmed-article:17438033 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17438033 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:17438033 | lifeskim:mentions | umls-concept:C0023238 | lld:lifeskim |
| pubmed-article:17438033 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:17438033 | lifeskim:mentions | umls-concept:C0033739 | lld:lifeskim |
| pubmed-article:17438033 | lifeskim:mentions | umls-concept:C1383501 | lld:lifeskim |
| pubmed-article:17438033 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:17438033 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
| pubmed-article:17438033 | lifeskim:mentions | umls-concept:C0870509 | lld:lifeskim |
| pubmed-article:17438033 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:17438033 | pubmed:dateCreated | 2007-6-20 | lld:pubmed |
| pubmed-article:17438033 | pubmed:abstractText | The Legionella pneumophila-containing phagosome evades endocytic fusion and intercepts endoplasmic reticulum (ER)-to-Golgi vesicle traffic, which is believed to be mediated by the Dot/Icm type IV secretion system. Although phagosomes harboring dot/icm mutants are thought to mature through the endosomal-lysosomal pathway, colocalization studies with lysosomal markers have reported contradictory results. In addition, phagosomes harboring the dot/icm mutants do not interact with endocytosed materials, which is inconsistent with maturation of the phagosomes in the endosomal-lysosomal pathway. Using multiple strategies, we show that the dot/icm mutants defective in the Dot/Icm structural apparatus are unable to maintain the integrity of their phagosomes and escape into the cytoplasm within minutes of entry into various mammalian and protozoan cells in a process independent of the type II secretion system. In contrast, mutants defective in cytoplasmic chaperones of Dot/Icm effectors and rpoS, letA/S, and letE regulatory mutants are all localized within intact phagosomes. Importantly, non-dot/icm L. pneumophila mutants whose phagosomes acquire late endosomal-lysosomal markers are all located within intact phagosomes. Using high-resolution electron microscopy, we show that phagosomes harboring the dot/icm transporter mutants do not fuse to lysosomes but are free in the cytoplasm. Inhibition of ER-to-Golgi vesicle traffic by brefeldin A does not affect the integrity of the phagosomes harboring the parental strain of L. pneumophila. We conclude that the Dot/Icm transporter is involved in maintaining the integrity of the L. pneumophila phagosome, independent of interception of ER-to-Golgi vesicle traffic, which is a novel function of type IV secretion systems. | lld:pubmed |
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| pubmed-article:17438033 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17438033 | pubmed:citationSubset | IM | lld:pubmed |
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