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See detailBacterial mastitis in the Azawak zebu breed at the Sahelian experimental station in Toukounous (Niger) : Identification and typing of Staphylococcus aureus
Issa, Ibrahim Abdoulkarim; Bada-Alambedji, Rianatou; Duprez, Jean-Noël ULg et al

in International Research Journal of Microbiology (2013), 4

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See detailBacterial mastitis in the Azawak zebu breed at the Sahelian experimental station in Toukounous (Niger): Identification and typing of Staphylococcus aureus
Issa Ibrahim, Abdoulkarim; Bada-Alambedji, Rlanatou; Duprez, Jean-Noel et al

in International Research Journal of Microbiology [=IRJM] (2013), 4(7), 168-178

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See detailBacterial peptidoglycan (murein) hydrolases.
Vollmer, Waldemar; Joris, Bernard ULg; Charlier, Paulette ULg et al

in FEMS Microbiology Reviews (2008), 32(2), 259-86

Most bacteria have multiple peptidoglycan hydrolases capable of cleaving covalent bonds in peptidoglycan sacculi or its fragments. An overview of the different classes of peptidoglycan hydrolases and ... [more ▼]

Most bacteria have multiple peptidoglycan hydrolases capable of cleaving covalent bonds in peptidoglycan sacculi or its fragments. An overview of the different classes of peptidoglycan hydrolases and their cleavage sites is provided. The physiological functions of these enzymes include the regulation of cell wall growth, the turnover of peptidoglycan during growth, the separation of daughter cells during cell division and autolysis. Specialized hydrolases enlarge the pores in the peptidoglycan for the assembly of large trans-envelope complexes (pili, flagella, secretion systems), or they specifically cleave peptidoglycan during sporulation or spore germination. Moreover, peptidoglycan hydrolases are involved in lysis phenomena such as fratricide or developmental lysis occurring in bacterial populations. We will also review the current view on the regulation of autolysins and on the role of cytoplasm hydrolases in peptidoglycan recycling and induction of beta-lactamase. [less ▲]

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See detailBacterial Peptidoglycans in Relation to the Membrane and the Mechanism of Action of Penicillin
Ghuysen, Jean-Marie ULg; Leyh-Bouille, Mélina; Perkins, Harold-R. et al

in Vanek, Z.; Hostalek, Z.; Cudlin, J. (Eds.) Genetics of industrial microorganisms. Bacteria (1973)

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See detailBacterial production and purification of recombinant human prolactin
Paris, N.; Rentier-Delrue, Françoise ULg; Defontaine, A. et al

in Biotechnology & Applied Biochemistry (1990), 12(4), 436-49

Escherichia coli cells transformed with a recombinant plasmid (pT7L) containing the coding sequence of human prolactin (hPrl) expressed a new protein. This protein, comigrating with human Prl on sodium ... [more ▼]

Escherichia coli cells transformed with a recombinant plasmid (pT7L) containing the coding sequence of human prolactin (hPrl) expressed a new protein. This protein, comigrating with human Prl on sodium dodecyl sulfate (SDS)-polyacrylamide gels, represented 50% of the total bacterial extract. Immunoprecipitation of [35S]methionine-labeled bacterial lysate with a rabbit antiserum to hPrl followed by SDS-polyacrylamide gel electrophoresis (PAGE) analysis showed that the major component had a Mr identical to that of standard hPrl. The majority of the recombinant hPrl (r-hPrl) accumulated in inclusion bodies. Analysis of these inclusion bodies by SDS-PAGE under nonreducing conditions showed that they are composed mostly of fully reduced monomers. Solubilization of the inclusion bodies and protein denaturation were performed in 8 M urea. Refolding during the renaturation procedure was confirmed by SDS-PAGE under nonreducing conditions. r-hPrl was further purified by gel permeation chromatography on a fast protein liquid chromatography column. More than 95% of the molecules were recovered as oxidized monomeric forms. The refolded molecule was tested for its bioactivity in the Nb2 lymphoma mitogenic assay. The dose-response curves obtained with either r-hPrl or pituitary-derived hPrl showed a complete parallelism. Furthermore, Nb2 cell proliferation was completely blocked by addition of hPrl antiserum to both preparations. Recombinant hPrl is identical to natural hPrl except for an additional methionine group at the amino terminal end. [less ▲]

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See detailBacterial protein synthesis in the pig's large intestine varies according to the fermented non-starch polysaccharides.
Bindelle, Jérôme ULg; Leterme, Pascal; Destain, Jean-Pierre ULg et al

in Journal of Animal Science (2007), 85(Suppl. 2), 114-115

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See detailBacterial symbionts and mineral deposits in the branchial chamber of the hydrothermal vent shrimp Rimicaris exoculata: relationship to moult cycle
Corbari, Laure; Zbinden, Magali; Cambon-Bonavita, Marie-Anne et al

in Aquatic Biology (2008), 1

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See detailBacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics
Ghuysen, Jean-Marie ULg; Frère, Jean-Marie ULg; Leyh-Bouille, Mélina et al

in Scandinavian Journal of Infectious Diseases (1984), 42

Wall peptidoglycan expansion in bacteria rests upon a cytoplasmic D-Ala: D-Ala ligase (ADP) which catalyses synthesis of a D-Ala-D-Ala dipeptide (with accompanying hydrolysis of one molecule of ATP) and a ... [more ▼]

Wall peptidoglycan expansion in bacteria rests upon a cytoplasmic D-Ala: D-Ala ligase (ADP) which catalyses synthesis of a D-Ala-D-Ala dipeptide (with accompanying hydrolysis of one molecule of ATP) and a set of DD-peptidases which utilize this D-Ala-D-Ala dipeptide--once it has been translocated at the outer face of the plasma membrane as the C-terminal portion of a disaccharide peptide unit--as carbonyl donor for transpeptidation and carboxypeptidation reactions (without additional energy expenditure). Four DD-peptidases have been selected which differ from each other with respect to the effects that amino compounds exert on the fate and rate of consumption of a D-Ala-D-Ala terminated amide carbonyl donor analogue. They serve as models to understand the different mechanisms by which the DD-peptidases perform catalysis and show widely varying responses to the action of beta-lactams, from extreme sensitivity to very high resistance. [less ▲]

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See detailBacterial Wall Peptidoglycans; Mecanism of Action of Penicillin
Ghuysen, Jean-Marie ULg; Leyh-Bouille, Mélina

in Genetics of Industrial Microorganisms : abstact book (1970)

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See detailBactericidal activity against Pseudomonas aeruginosa is acquired by cultured human monocyte-derived macrophages after uptake of myeloperoxidase.
Mathy-Hartert, M.; Deby, Ginette ULg; Melin, Pierrette ULg et al

in Experientia (1996), 52(2), 167-74

Myeloperoxidase (MPO) is an enzyme located within polymorphonuclear neutrophils capable of producing cytotoxic oxidant species that are particularly active against bacteria with polysaccharide capsules ... [more ▼]

Myeloperoxidase (MPO) is an enzyme located within polymorphonuclear neutrophils capable of producing cytotoxic oxidant species that are particularly active against bacteria with polysaccharide capsules. Pseudomonas aeruginosa (10(6) bacteria per 1ml) are killed within 1 h in vitro by a MPO/H2O2/C1- system (48mU=132ng of MPO). The question arose as to whether human macrophages would acquire cytotoxic activity when loaded with this enzyme. Monocytes were therefore isolated from human blood and cultured for up to ten days to induce maturation to macrophages. These cells lost endogenous MPO within five days while H2O2 production in response to stimulation by phorbol myristate acetate (10(-6)M) decreased to 23% within ten days. On the other hand, their capacity to take up exogenous MPO increased fourfold from day three to day ten. Human macrophages cultured from eight days (when both H2O2 production and MPO uptake were sufficient) were therefore used to study the effects of MPO uptake on cytocidal activity against Pseudomonas aeruginosa. After a 1 h MPO loading period, macrophages (5X10(5) cells per ml) were incubated in the presence of bacteria (0.5 to 2X10(6) bacteria per ml) for 2 h at 37 degrees C. At a bacteria/macrophage ratio of 1, only 34.8+/-7.0% of bacteria survived (compared to killing by non-loaded macrophages), while 74.4+/-9.3% survived at a ratio of 4. From these results, we conclude that loading macrophages with exogenous MPO could enhance their microbicidal activity, suggesting a potentially useful therapeutic application. [less ▲]

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See detailLes bactéries lactiques, une aide alimentaire.
Thonart, Philippe ULg; Roblain, D.

in Mellitus Magazine (1992), 3

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See detailBacteriochlorin a activated oxygen forms production: a ESR and a laser flash photolysis study
Hoebeke, Maryse ULg; Lindqvist, L.; van de Vorst, A.

Conference (1996)

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See detailBacteriocin Activity By Lactobacillus Curvatus Cwbi-B28 To Inactivate Listeria Monocytogenes In Cold-Smoked Salmon During 4 Degrees C Storage
Ghalfi, H.; Allaoui, A.; Destain, Jacqueline ULg et al

in Journal of Food Protection (2006), 69(5),

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See detailBacteriocin producers from traditional food products
Diop, Michel Bakar; Dubois Dauphin, Robin ULg; Tine, Emmanuel et al

in Biotechnologie, Agronomie, Société et Environnement = Biotechnology, Agronomy, Society and Environment [=BASE] (2007), 11(4), 275-281

A total of 220 strains of LAB isolated from 32 samples of traditional fermented food from Senegal were screened for bacteriocin production. Two bacteriocin producers, Lactococcus lactis subsp. lactis and ... [more ▼]

A total of 220 strains of LAB isolated from 32 samples of traditional fermented food from Senegal were screened for bacteriocin production. Two bacteriocin producers, Lactococcus lactis subsp. lactis and Enterococcus faecium, were identifi ed from 12 bacteriocin-producing isolates on the basis of phenotypic analyses and 16S rDNA sequence. Both bacteriocins produced by new isolates show antimicrobial activity against Listeria monocytogenes and Bacillus coagulans whereas only that produced by Lactococcus lactis has an activity against Bacillus cereus. Bacteriocin-producing Lactococcus lactis strains were found in a variety of traditional foods indicating a high potential of growth of this strain in variable ecological complex environment. Partial 16S rDNA of the two bacteriocin producers obtained in this study has been registered to Genbank databases under the accession number AY971748 for Lactococcus lactis subsp. lactis (named CWBI-B1410) and AY971749 for Enterococcus faecium (named CWBI-B1411). The new bacteriocin-producing Lactococcus lactis subsp. lactis strain has been selected for identification and application of the bacteriocin to food preservation. [less ▲]

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See detailLes bactériocines des bactéries lactiques : caractéristiques et intérêts pour la bioconservation des produits alimentaires
Dortu, C.; Thonart, Philippe ULg

in Biotechnologie, Agronomie, Société et Environnement = Biotechnology, Agronomy, Society and Environment [=BASE] (2009), 13(1), 349-356

Bacteriocins from lactic acid bacteria: interest for food products biopreservation. Bacteriocins from lactic acid bacteria are low molecular weight antimicrobial peptides. They have inhibitory activity ... [more ▼]

Bacteriocins from lactic acid bacteria: interest for food products biopreservation. Bacteriocins from lactic acid bacteria are low molecular weight antimicrobial peptides. They have inhibitory activity against the bacteria that are closed related to the producer strains and a narrow inhibitory spectrum. Nevertheless, most of them have activity against some food-born pathogenic bacteria as Listeria monocytogenes. The application of bacteriocins or bacteriocin producing lactic acid bacteria in food products to inhibit pathogenic or food-spoilage bacteria has then been suggested. This review focuses on the classification, structure, function, mode of action, biosynthesis and current food applications of bacteriocins from lactic acid bacteria. [less ▲]

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See detailBacteriogical evidence of leptospira infetion in wild mammals from Azores archipelago, Portugal (short report)
Collares Pereira, Margarida; Santos Reis, Margarida; Oom, Maria do Mar et al

in Vie et milieu (1996), 46(3-4), 380-381

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See detailBacteriological assessment of smoked game meat in Lubumbashi, D.R.C.
Kabwang a Mpalang, Rosette; Kakubu a Mpalang, Mireille; Mukeng Kaut, Clarence et al

in Biotechnologie, Agronomie, Société et Environnement = Biotechnology, Agronomy, Society and Environment [=BASE] (2013), 17

The bacteriological quality of smoked game meat in Lubumbashi has not been studied much to date. The present study focused on the analysis of 182 samples of smoked game meat from three species, Syncerus ... [more ▼]

The bacteriological quality of smoked game meat in Lubumbashi has not been studied much to date. The present study focused on the analysis of 182 samples of smoked game meat from three species, Syncerus caffer (n = 63), Phacochoerus aethiopicus (n = 60) and Sylvicapra grimmia (n = 59), sold at retail outlets in Lubumbashi. The isolation of Escherichia coli from 81.3% of samples (mean 4.87 ± 0.6 log10 CFU.g-1 of sample) confirms significant faecal contamination of smoked game meat. The study has determined by culture prevalences of 0.0%, 4.3% [CI95% 1.4-7.4], 3.8% [CI95% 1.1-6.6] and 14.2% [CI95% 9.2-19.4] respectively for Shiga toxigenic Escherichia coli (STEC), Salmonella spp., Campylobacter jejuni and Campylobacter coli. Using Polymerase Chain Reaction, these prevalences were of 2.2% [IC95% 0.1-4.3], 6.0% [IC95% 2.6-9.5], 3.8% [IC95% 1.1-6.6] and 15.9% [IC95% 10.6-21.3] respectively for STEC, Salmonella spp., C. jejuni and C. coli. Syncerus caffer was established as a potential vehicle of STEC carrying stx1 gene (3.2%), stx2 gene (1.6%) and the combination of stx2 and eae genes (1.6%). On the basis of these data, we suggested the need for developing monitoring plans of the production, preparation, handling and distribution of smoked game meat in Lubumbashi. [less ▲]

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See detailBacteriological identification and antibiotic sensitivity testing
Mainil, Jacques ULg; Menozzi, M.; Pelkonen, S. et al

in Mainil, Jacques (Ed.) Genus Clostridium - Clostridia in medical, veterinary and food microbiology : Diagnosis and typing (2006)

Detailed reference viewed: 3 (0 ULg)