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Using proteomics to identify host cell interaction partners for VgrG and IglJ
M. Proksova, H. Rehulkova, P. Rehulka, C. Lays, J. Lenco, J. Stulik
Language English Country Great Britain
Document type Journal Article, Research Support, Non-U.S. Gov't
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- MeSH
- Adaptive Immunity physiology MeSH
- Bacterial Proteins metabolism MeSH
- Francisella tularensis metabolism MeSH
- Genomic Islands * MeSH
- Mass Spectrometry MeSH
- Immunity, Innate physiology MeSH
- Proteomics MeSH
- Gene Expression Regulation, Bacterial * MeSH
- Tularemia microbiology MeSH
- Virulence MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Francisella tularensis is a highly virulent intracellular bacterium and the causative agent of tularemia. The disease is characterized by the suboptimal innate immune response and consequently by the impaired adaptive immunity. The virulence of this pathogen depends on proteins encoded by a genomic island termed the Francisella Pathogenicity Island (FPI). However, the precise biological roles of most of the FPI-encoded proteins remain to be clarified. In this study, we employed stable isotope labeling by amino acids in cell culture (SILAC) in combination with affinity protein purification coupled with liquid chromatography-mass spectrometry to identify potential protein-effector binding pairs for two FPI virulence effectors IglJ and VgrG. Our results may indicate that while the IglJ protein interactions primarily affect mitochondria, the VgrG interactions affect phagosome and/or autophagosome biogenesis via targeting components of the host's exocyst complex.
CIRI International Center for Infectiology Research Inserm U1111 UMR5308 CNRS Lyon France
Faculty of Pharmacy Charles University Hradec Kralove Czech Republic
References provided by Crossref.org
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