The Experts below are selected from a list of 18 Experts worldwide ranked by ideXlab platform
Hazel M. Mitchell - One of the best experts on this subject based on the ideXlab platform.
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Pathogenic Potential of Campylobacter ureolyticus
Infection and Immunity, 2011Co-Authors: Jose A. Burgos-portugal, Nadeem O. Kaakoush, Mark J. Raftery, Hazel M. MitchellAbstract:The recent detection and isolation of the aflagellate Campylobacter ureolyticus (previously known as Bacteroides ureolyticus) from intestinal biopsy specimens and fecal samples of children with newly diagnosed Crohn's disease led us to investigate the pathogenic potential of this Bacterium. Adherence and gentamicin protection assays were employed to quantify the levels of Adherence to and invasion into host cells. C. ureolyticus UNSWCD was able to adhere to the Caco-2 intestinal epithelial cell line with a value of 5.341% ± 0.74% but was not able to invade the Caco-2 cells. The addition of two proinflammatory cytokines, tumor necrosis factor alpha (TNF-α) and gamma interferon (IFN-γ), to the cell line did not affect attachment or invasion, with attachment levels being 4.156% ± 0.61% (P = 0.270) for TNF-α and 6.472% ± 0.61% (P = 0.235) for IFN-γ. Scanning electron microscopy visually confirmed attachment and revealed that C. ureolyticus UNSWCD colonizes and adheres to intestinal cells, inducing cellular damage and microvillus degradation. Purification and identification of the C. ureolyticus UNSWCD secretome detected a total of 111 proteins, from which 29 were bioinformatically predicted to be secretory proteins. Functional classification revealed three putative virulence and colonization factors: the surface antigen CjaA, an outer membrane fibronectin binding protein, and an S-layer RTX toxin. These results suggest that C. ureolyticus has the potential to be a pathogen of the gastrointestinal tract.
Christiane Forestier - One of the best experts on this subject based on the ideXlab platform.
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Aggregative Adherence of Klebsiella pneumoniae to human intestine-407 cells.
Infection and Immunity, 1995Co-Authors: S Favre-bonte, A Darfeuille-michaud, Christiane ForestierAbstract:Aggregative adhesion of Klebsiella pneumoniae LM3 to Intestine-407 (Int-407) cells was studied. Adhesive capacities were affected by the bacterial growth phase (with a maximum of Adherence obtained during the exponential phase), temperature, multiplicity of infection, and length of incubation with Int-407 cells. Adhesion occurred through a cytochalasin D-sensitive process and was greatly reduced after treatment of Int-407 with cycloheximide, indicating that aggregative adhesion requires active participation of Int-407 cells. Transmission electron microscopy revealed that adherent bacteria were surrounded by a capsule-like material, apparently involved in both Bacterium-Int-407 cell and Bacterium-Bacterium Adherence. Examination with a scanning electron microscope showed interactions of intestinal cell microvilli with bacteria and formation in 3 h of a fibrous network within and around the bacterial clusters. We speculate that aggregative adhesion of K. pneumoniae mediated by a capsule-like extracellular material might explain the persistence of these strains inside the host gastrointestinal tract.
Jose A. Burgos-portugal - One of the best experts on this subject based on the ideXlab platform.
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Pathogenic Potential of Campylobacter ureolyticus
Infection and Immunity, 2011Co-Authors: Jose A. Burgos-portugal, Nadeem O. Kaakoush, Mark J. Raftery, Hazel M. MitchellAbstract:The recent detection and isolation of the aflagellate Campylobacter ureolyticus (previously known as Bacteroides ureolyticus) from intestinal biopsy specimens and fecal samples of children with newly diagnosed Crohn's disease led us to investigate the pathogenic potential of this Bacterium. Adherence and gentamicin protection assays were employed to quantify the levels of Adherence to and invasion into host cells. C. ureolyticus UNSWCD was able to adhere to the Caco-2 intestinal epithelial cell line with a value of 5.341% ± 0.74% but was not able to invade the Caco-2 cells. The addition of two proinflammatory cytokines, tumor necrosis factor alpha (TNF-α) and gamma interferon (IFN-γ), to the cell line did not affect attachment or invasion, with attachment levels being 4.156% ± 0.61% (P = 0.270) for TNF-α and 6.472% ± 0.61% (P = 0.235) for IFN-γ. Scanning electron microscopy visually confirmed attachment and revealed that C. ureolyticus UNSWCD colonizes and adheres to intestinal cells, inducing cellular damage and microvillus degradation. Purification and identification of the C. ureolyticus UNSWCD secretome detected a total of 111 proteins, from which 29 were bioinformatically predicted to be secretory proteins. Functional classification revealed three putative virulence and colonization factors: the surface antigen CjaA, an outer membrane fibronectin binding protein, and an S-layer RTX toxin. These results suggest that C. ureolyticus has the potential to be a pathogen of the gastrointestinal tract.
S Favre-bonte - One of the best experts on this subject based on the ideXlab platform.
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Aggregative Adherence of Klebsiella pneumoniae to human intestine-407 cells.
Infection and Immunity, 1995Co-Authors: S Favre-bonte, A Darfeuille-michaud, Christiane ForestierAbstract:Aggregative adhesion of Klebsiella pneumoniae LM3 to Intestine-407 (Int-407) cells was studied. Adhesive capacities were affected by the bacterial growth phase (with a maximum of Adherence obtained during the exponential phase), temperature, multiplicity of infection, and length of incubation with Int-407 cells. Adhesion occurred through a cytochalasin D-sensitive process and was greatly reduced after treatment of Int-407 with cycloheximide, indicating that aggregative adhesion requires active participation of Int-407 cells. Transmission electron microscopy revealed that adherent bacteria were surrounded by a capsule-like material, apparently involved in both Bacterium-Int-407 cell and Bacterium-Bacterium Adherence. Examination with a scanning electron microscope showed interactions of intestinal cell microvilli with bacteria and formation in 3 h of a fibrous network within and around the bacterial clusters. We speculate that aggregative adhesion of K. pneumoniae mediated by a capsule-like extracellular material might explain the persistence of these strains inside the host gastrointestinal tract.
S M Dabo - One of the best experts on this subject based on the ideXlab platform.
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Binding of Bartonella henselae to extracellular molecules: identification of potential adhesins.
Microbial Pathogenesis, 2006Co-Authors: S M Dabo, A W Confer, J.t. Saliki, Burt E. AndersonAbstract:Bartonella henselae, the etiologic agent of cat scratch disease, bacillary angiomatosis and other clinical syndromes initiates infection through a trauma or wound to the skin suggesting involvement of extracellular matrix molecules. We have demonstrated in this study that B. henselae bound strongly fibronectin, collagen IX and X, but comparatively less laminin and collagen IV. B. henselae bound primarily the N- and C-terminal heparin (Hep-1 and Hep-2, respectively) and the gelatin-binding domains of fibronectin (Fn) but not the cell-binding domain. Binding to the Hep-binding domain was significantly inhibited by Hep suggesting common binding sites on the Fn molecule. Furthermore, glycosaminoglycans-mediated binding of B. henselae to soluble Fn showed that Hep but not dextran sulfate inhibited the Bacterium binding to Fn. Unlike Fn, B. henselae bound strongly vitronectin only in the presence of Hep or dextran sulfate. Also, the binding of B. henselae to host cells could be inhibited by anti-B. henselae surface-reactive antibodies, the exogenous Fn or the anti-Fn polyclonal antibodies. Ligand blots, batch affinity purification and MALDI-TOF peptide fingerprinting identified B. henselae Pap31, Omp43 and Omp89 as the three major putative Fn-binding proteins (FnBPs) in B. henselae outer membrane proteins. We hypothesized that B. henselae wound associated infections involved interactions with extracellular matrix molecules. Taken together, the above data suggest that interactions between B. henselae and ECM molecules such as Fn may play an important role in the Bacterium Adherence to and invasion of host cells.
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Adherence of Pasteurella multocida to fibronectin.
Veterinary microbiology, 2005Co-Authors: S M Dabo, A W Confer, S D HartsonAbstract:For many pathogens, Adherence and/or invasion involve association with host extracellular matrix molecules, such as fibronectin (Fn). Pasteurella multocida was found to bind significantly to Fn and collagen type IX but not to laminin and collagen types IV and X. The binding of P. multocida to Fn was dose-dependent and was inhibited by heparin (Hep). Removal of polysaccharide capsule enhanced the binding capacity of the Bacterium to Fn and inhibition by Hep. Protease treatment of bacteria decreased binding, implicating surface protein(s) as adhesive components. Investigation of the binding domain(s) of P. multocida on the Fn molecule revealed preferential binding to the N-terminal Hep-binding domain of Fn but not to the carboxyl-terminal Hep-binding domain. Furthermore, Fn, and anti-Fn antibodies inhibited P. multocida Adherence to Madin-Darby bovine kidney cells, suggesting the involvement of Fn in the Bacterium Adherence to host cells. Ligand blotting, batch affinity purification and MALDI-TOF mass spectrometry implicated several proteins as putative adhesins of P. multocida in the Fn-mediated Adherence. Taken together, the data suggest that P. multocida-Fn interaction may play a role in the Bacterium Adherence to host cells, and this may be mediated by bacterial surface proteins with preferential affinity for the Hep-1 binding domain of Fn.
