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10.1073/pnas.1615771114 http://scihub22266oqcxt.onion/10.1073/pnas.1615771114 C5338555!5338555 !28193861     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28193861 &cmd=llinks): Failed to open stream: HTTP request failed! 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Galectin-3 directs antimicrobial guanylate binding proteins to vacuoles furnished with bacterial secretion systems |pdf=|usr=}}{{28193861 }} gab.com Text Galectin-3 directs antimicrobial guanylate binding proteins to vacuoles furnished with bacterial secretion systems JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28193861 #FOAvip Many invasive bacteria establish pathogen-containing vacuoles (PVs) as intracellular niches for microbial growth. Immunity to these infections is dependent on the ability of host cells to recognize PVs as targets for host defense. The delivery of several host defense proteins to PVs is controlled by IFN-inducible guanylate binding proteins (GBPs), which themselves dock to PVs through poorly characterized mechanisms. Here, we demonstrate that GBPs detect the presence of bacterial protein secretion systems as "patterns of pathogenesis" associated with PVs. We report that the delivery of GBP2 to Legionella-containing vacuoles is dependent on the bacterial Dot/Icm secretion system, whereas the delivery of GBP2 to Yersinia-containing vacuoles (YCVs) requires hypersecretion of Yersinia translocon proteins. We show that the presence of bacterial secretion systems directs cytosolic carbohydrate-binding protein Galectin-3 to PVs and that the delivery of GBP1 and GBP2 to Legionella-containing vacuoles or YCVs is substantially diminished in Galectin-3-deficient cells. Our results illustrate that insertion of bacterial secretion systems into PV membranes stimulates Galectin-3-dependent recruitment of antimicrobial GBPs to PVs as part of a coordinated host defense program. Twit Text FOAVip Galectin-3 directs antimicrobial guanylate binding proteins to vacuoles furnished with bacterial secretion systems ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28193861 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28193861 #FOAvip English Wikipedia <ref>{{Cite pmid|28193861 }}</ref> Galectin-3 directs antimicrobial guanylate binding proteins to vacuoles furnished with bacterial secretion systems #MMPMID28193861 Feeley EM ; Pilla-Moffett DM ; Zwack EE ; Piro AS ; Finethy R ; Kolb JP ; Martinez J ; Brodsky IE ; Coers J Proc Natl Acad Sci U S A 2017[Feb]; 114 (9 ): E1698-E1706 PMID28193861 show ga Many invasive bacteria establish pathogen-containing vacuoles (PVs) as intracellular niches for microbial growth. Immunity to these infections is dependent on the ability of host cells to recognize PVs as targets for host defense. The delivery of several host defense proteins to PVs is controlled by IFN-inducible guanylate binding proteins (GBPs), which themselves dock to PVs through poorly characterized mechanisms. Here, we demonstrate that GBPs detect the presence of bacterial protein secretion systems as "patterns of pathogenesis" associated with PVs. We report that the delivery of GBP2 to Legionella-containing vacuoles is dependent on the bacterial Dot/Icm secretion system, whereas the delivery of GBP2 to Yersinia-containing vacuoles (YCVs) requires hypersecretion of Yersinia translocon proteins. We show that the presence of bacterial secretion systems directs cytosolic carbohydrate-binding protein Galectin-3 to PVs and that the delivery of GBP1 and GBP2 to Legionella-containing vacuoles or YCVs is substantially diminished in Galectin-3-deficient cells. Our results illustrate that insertion of bacterial secretion systems into PV membranes stimulates Galectin-3-dependent recruitment of antimicrobial GBPs to PVs as part of a coordinated host defense program. |Animals [MESH] |Anti-Infective Agents/*metabolism [MESH] |Bacterial Proteins/metabolism [MESH] |Bacterial Secretion Systems/*metabolism [MESH] |Carrier Proteins/metabolism [MESH] |Cells, Cultured [MESH] |GTP-Binding Proteins/*metabolism [MESH] |Galectin 3/*metabolism [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Legionella/metabolism [MESH] |Mice [MESH] |Mice, Inbred C57BL [MESH] |RAW 264.7 Cells [MESH] |Receptors, Cell Surface/metabolism [MESH]Galectin-3 directs antimicrobial guanylate binding proteins to vacuole(epmc).pdf DeepDyve Pubget Overpricing