20 research outputs found

    LA PRATIQUE DE L'ELECTROCONVULSIVOTHERAPIE

    No full text
    CHATENAY M.-PARIS 11-BU Pharma. (920192101) / SudocSudocFranceF

    Nutrient essentiality revisited

    Get PDF
    With increased understanding of the complex roles nutrients play within metabolic pathways, the purpose of this contribution is to explore the rationale for expanding the definitions and criteria for nutrient essentiality. A further objective was to develop three case study scenarios to probe issues surrounding the definition of essentiality using dietary fibre, plant sterols and polyphenols. Current definitions and criteria for essentiality were reviewed through an environmental scan of the scientific literature. Additionally, international regulatory bodies were asked whether the terms nutrient and/or essential nutrient are regulated in their respective jurisdictions. Regulatory bodies including the EFSA, the US FDA, HC and FSANZ were found not to currently possess regulated definitions for the term essential nutrient . Case studies examining fibre, plant sterols and polyphenols served as a means of presenting evidence for expanding the list of functional food constituents regarded as meeting criteria for essentiality. For each example, certain instances applied where these case study bioactives met criteria of essentiality. Thus, in order to reflect advances in current science, a series of non-classical compounds known to have bioactivity should be considered for their potential essentiality under certain situations

    Digestiveflora and Clostridium difficile. Experimental model for study of microbial ecology and pathogenicity

    No full text
    Boureau Hélène, Collignon Anne, Barc Marie-Claude, Kaijalainen Tuomo, Bourlioux Pierre. Flore digestive et Clostridium difficile . Modèle expérimental d’étude de l’écologie microbienne et de la pathogénicité. In: Bulletin de l'Académie Vétérinaire de France tome 147 n°1, 1994. pp. 55-62

    Phenotypic and Genotypic Diversity of the Flagellin Gene (fliC) among Clostridium difficile Isolates from Different Serogroups

    No full text
    Phenotypic and genotypic diversity of the flagellin gene (fliC) of Clostridium difficile was studied in 47 isolates from various origins belonging to the serogroups A, B, C, D, F, G, H, I, K, X, and S3. Electron microscopy revealed 17 nonflagellated strains and 30 flagellated strains. PCR and reverse transcription-PCR demonstrated that the flagellin gene was present in all strains and that the fliC gene was expressed in both flagellated and nonflagellated strains. Southern blotting showed the presence of only one copy of the gene and three different hybridization patterns. DNA sequence analysis of fliC from the strains belonging to serogroups C, D, and X, representative of each profile, disclosed great variability in the central domain, whereas the N- and C-terminal domains were conserved. The variability of the flagellin gene fliC was further studied in the isolates by PCR-restriction fragment length polymorphism (RFLP) analysis. Nine different RFLP groups were identified (I to IX), among which three (I, VII, and VIII) corresponded to numerous serogroups whereas the six others (II, III, IV, V, VI, and IX) belonged to a single serogroup. Flagellin gene RFLP analysis could constitute an additional typing method employable in conjunction with other typing methods currently available

    GroEL (Hsp60) of Clostridium difficile is involved in cell adherence.

    No full text
    International audiencePrevious results have demonstrated that adherence of Clostridium difficile to tissue culture cells is augmented by various stresses; this study focussed on whether the GroEL heat shock protein is implicated in this process. The 1940 bp groESL operon of C. difficile was isolated by PCR. The 1623 bp groEL gene is highly conserved between various C. difficile isolates as determined by RFLP-PCR and DNA sequencing, and the operon is present in one copy on the bacterial chromosome. The 58 kDa GroEL protein was expressed in Escherichia coli in fusion with glutathione S:-transferase and the fusion protein was purified from IPTG-induced bacterial lysates by affinity chromatography on glutathione-Sepharose. A polyclonal, monospecific antiserum was obtained for GroEL which established by immunoelectron microscopy, indirect immunofluorescence and immunoblot analysis that GroEL is released extracellularly after heat shock and can be surface associated. Cell fractionation experiments suggest that GroEL is predominantly cytoplasmic and membrane bound. GroEL-specific antibodies as well as the purified protein partially inhibited C. difficile cell attachment and expression of the protein was induced by cell contact, suggesting a role for GroEL in cell adherence
    corecore