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Registros recuperados: 5
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An important step in Listeria lipoprotein research Inra
Garcia-del Portillo, F.; Cossart, P..
Over the last 10 years, DNA sequences of more than 600 bacterial species have been deposited in databases and are now available to search any gene, motif, or regulatory sequence of interest. Although genome data are instrumental in phylogenetic analysis and in silico design of metabolic and regulatory networks, only a very small fraction of the information has been experimentally validated. A striking example is lipoproteins predicted from genome sequences. Despite the predominance of this class of surface proteins in bacteria (up to 0.5 to 8% of the proteome), very few of these proteins have been identified as lipoproteins by biochemical methods (19). In this issue of the Journal of Bacteriology, Baumgärtner et al. (2) report a systematic...
Tipo: Journal Article Palavras-chave: LIPOPROTEINE; LISTERIA MONOCYTOGENES; VIRULENCE; BACTERIE GRAM-POSITIVE; BACTERIE GRAM-NEGATIVE; BACTERIE PATHOGENE; ADN; SEQUENCE NUCLEOTIDIQUE; ANALYSE PHYLOGENETIQUE; REGULATION; PROTEINE; SURFACE CELLULAIRE; VIRULENCE; TECHNIQUE ANALYTIQUE; BIOCHIMIE.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009594c400a&uri=/notices/prodinra1/2009/11/
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Listeria InlB takes a different route to met Inra
Veiga, E.; Cossart, P..
InlB, a surface protein of the human bacterial pathogen Listeria monocytogenes, interacts with the receptor tyrosine kinase Met on host cells to enable bacterial invasion. In this issue, Niemann et al. (2007) provide the first structural evidence that InlB does not compete for the same interaction site on Met as the natural ligand HGF.
Tipo: Journal Article Palavras-chave: BACTERIE PATHOGENE; LISTERIA MONOCYTOGENES; PROTEINE; RECEPTEUR; TYROSINE KINASE; HOMME; SURFACE CELLULAIRE.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009a8e51aff&uri=/notices/prodinra1/2009/09/
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Listeria monocytogenes internalins bind to the human intestinal mucin MUC2 Inra
Lindén, S. K.; Bierne, H.; Sabet, C.; Png, C. W.; Florin, T. H.; McGuckin, M. A.; Cossart, P..
Listeria monocytogenes cross the intestinal barrier causing systemic infections with high mortality rates. Intestinal infection triggers release of intestinal mucus. We show that three L. monocytogenes internalins, InlB, InlC and InlJ all bound to MUC2 (the major component of intestinal mucus), but not to the cell surface mucin MUC1. Binding was strongest to InlB>InlC>InlJ (P < 0.001). Listerial internalins are characterized by their internalin domain, composed by leucine rich repeats (LRR) followed by an immunogloblin-like region. We report here that the internalin domain of the InlJ protein also bound MUC2, suggesting that an internalin domain is sufficient to bind to MUC2.
Tipo: Journal Article Palavras-chave: LISTERIA MONOCYTOGENES; BACTERIE; MUCINE; HOMME; INTESTIN; INFECTION; MUCUS; PROTEINE; LEUCINE; ACIDE AMINE; SURFACE CELLULAIRE; REACTION ANTIGENE ANTICORPS LISTERIA; LRRR; MUCIN; MUCUS; MUC2; MUC1.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20091b0155aa&uri=/notices/prodinra1/2010/10/
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Src, cortactin and Arp2/3 complex are required for E-cadherin-mediated internalization of Listeria into cells Inra
Sousa, S.; Cabanes, D.; Bougnères, L.; Lecuit, M.; Sansonetti, P.; Tran-Van-Nhieu, G.; Cossart, P..
Listeria monocytogenes is a food-borne pathogen able to invade non-phagocytic cells. InlA, a L. monocytogenes surface protein, interacts with human E-cadherin to promote bacterial entry. L. monocytogenes internalization is a dynamic process involving co-ordinated actin cytoskeleton rearrangements and host cell membrane remodelling at the site of bacterial attachment. Interaction between E-cadherin and catenins is required to promote Listeria entry, and for the establishment of adherens junctions in epithelial cells. Although several molecular factors promoting E-cadherin-mediated Listeria internalization have been identified, the proteins regulating the transient actin polymerization required at the bacterial entry site are unknown. Here we...
Tipo: Journal Article Palavras-chave: PROTEINE MICROBIENNE; LISTERIA MONOCYTOGENES; BACTERIE PATHOGENE; CADHERINE; PENETRATION CELLULAIRE; SURFACE CELLULAIRE; HOMME; MODELISATION; MEMBRANE CELLULAIRE.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20092f54e3ca&uri=/notices/prodinra1/2009/09/
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Successive post-translational modifications of E-cadherin are required for InlA-mediated internalization of Listeria monocytogenes Inra
Bonazzi, M.; Veiga, E.; Pizarro-Cerda, J.; Cossart, P..
Listeria monocytogenes surface proteins internalin (Inl)A and InlB interact with the junctional protein E-cadherin and the hepatocyte growth factor (HGF) receptor Met, respectively, on the surface of epithelial cells to mediate bacterial entry. Here we show that InlA triggers two successive E-cadherin posttranslationalmodifications, i.e. the Src-mediatedtyrosine phosphorylation of E-cadherin followed by its ubiquitination by the ubiquitin-ligase Hakai. E-cadherin ubiquitination induces the recruitment ofclathrin that is required for optimal bacterial internalization. We also show that the initial clustering of E-cadherin at the bacterial entry site requirescaveolin, a protein normally involved in clathrinindependent endocytosis. Strikingly...
Tipo: Journal Article Palavras-chave: BACTERIE PATHOGENE; LISTERIA MONOCYTOGENES; PROTEINE MICROBIENNE; CADHERINE; SURFACE CELLULAIRE; GLYCOPROTEINE; FACTEUR DE CROISSANCE; ENDOCYTOSE E-CADHERIN.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009b5349ff4&uri=/notices/prodinra1/2009/09/
Registros recuperados: 5
Primeira ... 1 ... Última
 

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