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Registros recuperados: 20 | |
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Velge, P.; Herler, M.; Johansson, J.; Roche, S.; Témoin, S.; Fedorov, A. A.; Gracieux, P.; Almo, S. C.; Goebel, W.; Cossart, P.. |
The sequencing of prfA, encoding the transcriptional regulator of virulence genes, in 26 low virulence field Listeria monocytogenes strains showed that eight strains exhibited the same single amino-acid substitution: PrfAK220T. These strains exhibited no expression of PrfA-regulated proteins and thus no virulence. This substitution inactivated PrfA, since expression of the PrfAK220T mutant gene in an EGDΔprfA strain did not restore the haemolytic and phosphatidylcholine phospholipase C activities, in contrast to the wild-type prfA gene. The substitution of the lysine at position 220 occurred in the helix αH. However, the data showed that the PrfAK220T protein is dimerized just as well as its wild-type counterpart, but does not bind to PrfA boxes.... |
Tipo: Journal Article |
Palavras-chave: LISTERIA MONOCYTOGENES; PROTEINE; FACTEUR DE VIRULENCE; BACTERIE PATHOGENE; ADN; SEQUENCE NUCLEOTIDIQUE; REGULATION; TRANSCRIPTION; VIRULENCE; EXPRESSION DES GENES; ACIDE AMINE; MUTATION; RT-PCR; ELECTROPHORESE; ENZYME; ARN POLYMERASE. |
Ano: 2007 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009c1895b3c&uri=/notices/prodinra1/2009/11/ |
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Bublitz, M.; Holland, C.; Sabet, C.; Reichelt, J.; Cossart, P.; Heinz, D. W.; Bierne, H.; Schubert, W. D.. |
We report on the crystal structure of the internalin domain of InlJ, a virulence-associated surface protein of Listeria monocytogenes, at 2.7-Å resolution. InlJ is a member of the internalin family of listerial cell surface proteins characterized by a common N-terminal domain. InlJ bears 15 leucine-rich repeats (LRRs), the same number as in InlA, the prototypical internalin family member. The LRRs of InlJ differ from those of other internalins by having 21, rather than 22, residues and by replacing 1 LRR defining hydrophobic residue with a conserved cysteine. These cysteines stack to form an intramolecular ladder and regular hydrophobic interactions in consecutive repeats. Analyzing the curvature, twist, and lateral bending angles of InlJ and... |
Tipo: Journal Article |
Palavras-chave: ACIDE AMINE; LEUCINE; CYSTEINE; PROTEINE; LISTERIA MONOCYTOGENES; BACTERIE PATHOGENE; VIRULENCE; SURFACE DE LA PROTEINE; SEQUENCE NUCLEOTIDIQUE LEUCINE-RICH REPEAT; CYSTEINE LADDER; ASPARAGINE LADDER; INTERNALIN; REPEAT GEOMETRY. |
Ano: 2008 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009da5e3652&uri=/notices/prodinra1/2010/11/ |
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Hamon, M. A.; Batsché, E.; Régnault, B.; Tham, T. N.; Seveau, S.; Muchardt, C.; Cossart, P.. |
Upon infection, pathogens reprogram host gene expression. In eukaryotic cells, genetic reprogramming is induced by the concerted activation/repression of transcription factors and various histone modifications that control DNA accessibility in chromatin. We report here that the bacterial pathogen Listeria monocytogenes induces a dramatic dephosphorylation of histone H3 as well as a deacetylation of histone H4 during early phases of infection. This effect is mediated by the major listerial toxin listeriolysin O in a pore-forming-independent manner. Strikingly, a similar effect also is observed with other toxins of the same family, such as Clostridium perfringens perfringolysin and Streptococcus pneumoniae pneumolysin. The decreased levels of... |
Tipo: Journal Article |
Palavras-chave: HISTONE; BACTERIE PATHOGENE; AGENT PATHOGENE; EXPRESSION DES GENES; ADN; SEQUENCE NUCLEOTIDIQUE; INFECTION; TRANSCRIPTION; REGULATION; EUCARYOTE; PHOSPHORE; DEPHOSPHORYLATION EPIGENETIC; LISTERIA MONOCYTOGENES; PATHOGENESIS . |
Ano: 2007 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009b0bc6f33&uri=/notices/prodinra1/2009/11/ |
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Mandin, P.; Repoila, F.; Vergassola, M.; Geissmann, T.; Cossart, P.. |
To identify noncoding RNAs (ncRNAs) in the pathogenic bacterium Listeria monocytogenes, we analyzed the intergenic regions (IGRs) of strain EGD-e by in silico-based approaches. Among the twelve ncRNAs found, nine are novel and specific to the Listeria genus, and two of these ncRNAs are expressed in a growth-dependent manner. Three of the ncRNAs are transcribed in opposite direction to overlapping open reading frames (ORFs), suggesting that they act as antisense on the corresponding mRNAs. The other ncRNA genes appear as single transcription units. One of them displays five repeats of 29 nucleotides. Five of these new ncRNAs are absent from the non-pathogenic species L. innocua, raising the possibility that they might be involved in... |
Tipo: Journal Article |
Palavras-chave: BACTERIE PATHOGENE; PROTEINE BACTERIENNE; LISTERIA MONOCYTOGENES; VIRULENCE; ARN; ARN MESSAGER; TRANSCRIPTION; TECHNIQUE ANALYTIQUE; SEQUENCE NUCLEOTIDIQUE; GENE ANTISENS; VIRULENCE. |
Ano: 2007 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009f388695&uri=/notices/prodinra1/2009/11/ |
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Veiga, E.; Guttman, J. A.; Bonazzi, M.; Boucrot, E.; Toledo-Arana, A.; Lin, A. E.; Enninga, J.; Pizarro-Cerda, J.; Finlay, B. B.; Kirchhausen, T.; Cossart, P.. |
Infection by the bacterium Listeria monocytogenes depends on host cell clathrin. To determine whether this requirement is widespread, we analyzed infection models using diverse bacteria. We demonstrated that bacteria that enter cells following binding to cellular receptors (termed ‘‘zippering’’ bacteria) invade in a clathrin-dependent manner. In contrast, bacteria that inject effector proteins into host cells in order to gain entry (termed ‘‘triggering’’ bacteria) invade in a clathrin-independent manner. Strikingly, enteropathogenic Escherichia coli (EPEC) required clathrin to form actin-rich pedestals in host cells beneath adhering bacteria, even though this pathogen remains extracellular. Furthermore, clathrin accumulation preceded the actin... |
Tipo: Journal Article |
Palavras-chave: BACTERIE PATHOGENE; LISTERIA MONOCYTOGENE; INFECTION BACTERIENNE; PROTEINE; CLATHRINE; ESCHERICHIA COLI; INFECTION; MODELE; ADHERENCE. |
Ano: 2007 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20094c6cd329&uri=/notices/prodinra1/2009/09/ |
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Lambrechts, A.; Gevaert, K.; Cossart, P.; Vandekerckhove, J.; van Troys, M.. |
Listeria monocytogenes is a master of mimicry that uses the host cell actin system both to move within the cytoplasm of infected cells and for cell-to-cell spread. Recent studies of Listeria and similarly acting pathogens have generated leaps in our understanding of the actinbased force producing machinery. This machinery is essential for most motile properties of cells, not least for cell migration. In a minimal configuration, it consists of the Arp2/3-complex, Ena–VASP proteins, cofilin, capping protein and a nucleation-promoting factor. In this review, we discuss current models of pseudopodial protrusions and describe how the road to more complex models lies open and is already paved by recent studies using Listeria-based biomimetic... |
Tipo: Journal Article |
Palavras-chave: LISTERIA MONOCYTOGENES; MOTILITE; ACTINE; PROTEINE; BACTERIE PATHOGENE; INFECTION; CYTOPLASME; POUVOIR PATHOGENE; ACTINE; MODELISATION; PROTEINE; EXPRESSION DES GENES. |
Ano: 2008 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD200990b263f3&uri=/notices/prodinra1/2010/11/ |
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Birmingham, C. L.; Canadien, V.; Gouin, E.; Troy, E. B.; Yoshimori, T.; Cossart, P.; Higgins, D.; Brumell, J. H.. |
Listeria monocytogenes is an intracellular pathogen that is able to colonize the cytosol of macrophages. Here we examined the interaction of this pathogen with autophagy, a host cytosolic degradative pathway that constitutes an important component of innate immunity towards microbial invaders. L. monocytogenes infection induced activation of the autophagy system in macrophages. At 1 h post infection (p.i.), a population of intracellular bacteria (~37%) colocalized with the autophagy marker LC3. These bacteria were within vacuoles and were targeted by autophagy in an LLO-dependent manner. At later stages in infection (by 4 h p.i.), the majority of L. monocytogenes escaped into the cytosol and rapidly replicated. At these times, less than 10% of... |
Tipo: Journal Article |
Palavras-chave: LISTERIA MONOCYTOGENES; PATHOGENE INTRACELLULAIRE; BACTERIE PATHOGENE; INFECTION; MACROPHAGE; AUTOPHAGE; CYTOSOL; POUVOIR PATHOGENE; VIRULENCE; PHOSPHOLIPASE; ENZYME; BACTERIE GRAM POSITIF. |
Ano: 2007 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20096e981c45&uri=/notices/prodinra1/2009/09/ |
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Hain, T.; Chatterjee, S. S.; Ghai, R.; Kuenne, C. T.; Billion, A.; Steinweg, C.; Domann, E.; Kärst, U.; Jänsch, L.; Wehland, J.; Eisenreich, W.; Bacher, A.; Joseph, B.; Schär, J.; Kreft, J.; Klumpp, J.; Loessner, M. J.; Dorscht, J.; Neuhaus, K.; Fuchs, T. M.; Scherer, S.; Doumith, M.; Jacquet, C.; Martin, P.; Cossart, P.; Rusniock, C.; Glaser, P.; Buchrieser, C.; Goebel, W.; Chakraborty, T.. |
This review provides an overview of recent progress in the exploration of genomic, transcriptomic, and proteomic data in Listeria spp. to understand genome evolution and diversity, as well as physiological aspects of metabolism utilized by the bacteria when growing in diverse and varied environments. |
Tipo: Journal Article |
Palavras-chave: LISTERIA; BACTERIE; GENOME; ADN; GENOMIQUE; TRANSCRIPTOMIQUE; PROTEOMIQUE; METABOLISME; IMPACT DE L'ENVIRONNEMENT; DIVERSITE; EXPRESSION DES GENES; BACTERIE PATHOGENE; PATHOGENICITE; VARIABILITE LISTERIA; GENOMIC; TRANSCRIPTOMIC; PROTEOMIC; BACTERIOPHAGE; METABOLISM. |
Ano: 2007 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20097b41fd4e&uri=/notices/prodinra1/2009/12/ |
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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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Registros recuperados: 20 | |
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