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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 16
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pubmed:dateCreated |
2007-8-10
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pubmed:abstractText |
Mycobacterium tuberculosis evades the innate antimicrobial defenses of macrophages by inhibiting the maturation of its phagosome to a bactericidal phagolysosome. Despite intense studies of the mycobacterial phagosome, the mechanism of mycobacterial persistence dependent on prolonged phagosomal retention of the coat protein coronin-1 is still unclear. The present study demonstrated that several mycobacterial proteins traffic intracellularly in M. bovis BCG-infected cells and that one of them, with an apparent subunit size of M(r) 50,000, actively retains coronin-1 on the phagosomal membrane. This protein was initially termed coronin-interacting protein (CIP)50 and was shown to be also expressed by M. tuberculosis but not by the non-pathogenic species M. smegmatis. Cell-free system experiments using a GST-coronin-1 construct showed that binding of CIP50 to coronin-1 required cholesterol. Thereafter, mass spectrometry sequencing identified mycobacterial lipoamide dehydrogenase C (LpdC) as a coronin-1 binding protein. M. smegmatis over-expressing Mtb LpdC protein acquired the capacity to maintain coronin-1 on the phagosomal membrane and this prolonged its survival within the macrophage. Importantly, IFNgamma-induced phagolysosome fusion in cells infected with BCG resulted in the dissociation of the LpdC-coronin-1 complex by a mechanism dependent, at least in part, on IFNgamma-induced LRG-47 expression. These findings provide further support for the relevance of the LpdC-coronin-1 interaction in phagosome maturation arrest.
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pubmed:commentsCorrections |
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9533
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pubmed:author |
pubmed-author:Av-GayYossefY,
pubmed-author:BachHoracioH,
pubmed-author:DeghmaneAla-EddineAE,
pubmed-author:HmamaZakariaZ,
pubmed-author:ItohSaotomoS,
pubmed-author:LoRaymondR,
pubmed-author:NoubirSanaaS,
pubmed-author:SendideKhalidK,
pubmed-author:SoualhineHafidH,
pubmed-author:SoulhineHafidH,
pubmed-author:TalalAminaA,
pubmed-author:TamAndreaA,
pubmed-author:ToyoshimaSatoshiS
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
120
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2796-806
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:17652161-Amino Acid Sequence,
pubmed-meshheading:17652161-Animals,
pubmed-meshheading:17652161-Bacterial Proteins,
pubmed-meshheading:17652161-Cholesterol,
pubmed-meshheading:17652161-Dihydrolipoamide Dehydrogenase,
pubmed-meshheading:17652161-GTP-Binding Proteins,
pubmed-meshheading:17652161-Interferon-gamma,
pubmed-meshheading:17652161-Macrophages,
pubmed-meshheading:17652161-Mice,
pubmed-meshheading:17652161-Microbial Viability,
pubmed-meshheading:17652161-Microfilament Proteins,
pubmed-meshheading:17652161-Molecular Sequence Data,
pubmed-meshheading:17652161-Molecular Weight,
pubmed-meshheading:17652161-Mycobacterium bovis,
pubmed-meshheading:17652161-Mycobacterium smegmatis,
pubmed-meshheading:17652161-Mycobacterium tuberculosis,
pubmed-meshheading:17652161-Phagosomes,
pubmed-meshheading:17652161-Protein Binding,
pubmed-meshheading:17652161-Protein Transport,
pubmed-meshheading:17652161-Vacuoles
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pubmed:year |
2007
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pubmed:articleTitle |
Lipoamide dehydrogenase mediates retention of coronin-1 on BCG vacuoles, leading to arrest in phagosome maturation.
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pubmed:affiliation |
Division of Infectious Diseases, Department of Medicine, University of British Columbia, Vancouver Costal Health Institute, Vancouver, British Columbia, V5Z 3J5, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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