68 research outputs found
Observation of a 1750 MeV/c^2 Enhancement in the Diffractive Photoproduction of K^+K^-
Using the FOCUS spectrometer with photon beam energies between 20 and 160
\gev, we confirm the existence of a diffractively photoproduced enhancement in
at 1750 \mevcc with nearly 100 times the statistics of previous
experiments. Assuming this enhancement to be a single resonance with a
Breit-Wigner mass shape, we determine its mass to be
\mevcc and its width to be \mevcc. We find no
corresponding enhancement at 1750 \mevcc in , and again neglecting any
possible interference effects we place limits on the ratio . Our results are consistent with previous
photoproduction experiments, but, because of the much greater statistics,
challenge the common interpretation of this enhancement as the
seen in annihilation experiments.Comment: 10 pages, 5 figure
Role of mprF1 and mprF2 in the Pathogenicity of Enterococcus faecalis
Aujourd hui, Enterococcus faecalis est considéré comme l un des plus importants agents pathogènes causant des maladies nosocomiales. En raison de sa résistance innée et acquise aux antibiotiques, l identification de nouvelles cibles pour le traitement de cette bactérie est une grande priorité. Le facteur Multiple Peptide Résistance (MprF), qui a été décrit en premier chez Staphylococcus aureus, modifie le phosphatidylglycérol avec de la lysine et réduit ainsi la charge négative de l enveloppe cellulaire. Ceci a comme conséquence d augmenter la résistance aux peptides antimicrobiens cationiques (PAC). Deux gènes paralogues putatifs (mprF1 et mprF2) ont été identifiés chez E. faecalis par recherche BLAST en utilisant le gène décrit chez S. aureus. Une caractérisation de ces deux gènes d E. faecalis ainsi que des mécanismes conduisant à une résistance aux PAC, pourrait aider à développer des nouvelles stratégies thérapeutiques contre ce pathogène. Deux mutants de délétion et un double mutant ont été construits par recombinaison homologue chez E. faecalis. L analyse des phospholipides des membranes cytoplasmiques des deux mutants mprF1 et mprF2 par chromatographie sur couche mince a montré que seule l inactivation de mprF2 inhibe la synthèse de trois amino-phosphatidlyglycérol distincts (comme la Lysine-PG, l Alanine-PG et l Arginine-PG). De plus, le mutant mprF2 est également plus sensible aux PAC que la souche sauvage. La capacité de formation d un biofilm est généralement considérée comme un facteur important de virulence, ce qui est également le cas pour les entérocoques. Le mutant mprF2 montre une capacité accrue dans ce phénomène. Ceci semble être du à une augmentation de la concentration d ADN extracellulaire dans le biofilm formé par ce mutant. Curieusement, cette augmentation est indépendante d une autolyse. Le mutant mprF2 est également plus résistant à l opsonophagocytose. Cependant, le gène mprF2 ne joue aucun rôle dans les bactériémies de souris et les endocardites de rats.En revanche, aucun phénotype n a été trouvé pour un mutant mprF1 jusqu à présent. Cette mutation ne modifie ni la synthèse de l aminoacyl-PG en condition de laboratoire ni la résistance aux PAC et à l opsonophagocytose. Par conséquent, il semble que mprF2 soit le seul gène mprF fonctionnel chez E. faecalis. Néanmoins, contrairement à d autres bactéries, mprF2 ne semble pas être un facteur de virulence majeur pour cette espèce.Enterococcus faecalis is regarded nowadays as one of the most important nosocomial pathogens. Due to its innate and acquired resistance to antibiotics, identification of new targets for antimicrobial treatment of E. faecalis is a high priority. The multiple peptides resistance factor (MprF), which was first described in Staphylococcus aureus, modifies phosphatidylglycerol with lysine and reduces the negative charge of the membrane, thus increasing resistance to cationic antimicrobial peptides (CAMPs). Two putative mprF paralogs (mprF1 and mprF2) were identified in E. faecalis by Blast search using the well-described S. aureus gene as a lead. A better understanding of these two genes and mechanisms leads to enterococcal resistance to CAMPs might help designing therapeutic strategies against this bacteria. Two single deletion mutants and double mutant in E. faecalis were created by homologues recombination. Analysis of cell membrane phospholipids from both mutants by thin-layer chromatography showed that inactivation of mprF2 abolished the synthesis of three distinct amino-phosphatidylglycerol (mostly likely Lysin-PG, Alanine-PG and Argine-PG). The CAMPs testing assay demonstrated that the deletion mutant of mprF2 was more susceptible to CAMPs than the wild type. Biofilm formation is usually regarded as a virulence factor which provides an important way for enterococci to cause infections. Inactivation of mprF2 led to increase the biofilm formation which we showed that it was due to the accumulation of eDNA in the biofilm, but the release of eDNA is independent from autolysis. The mprF2 mutant was resistance to killing by opsonophagocytosis more than wild type. However, the mprF2 gene plays no role in bacteremia in mice and rat endocarditis. Our results showed that non polar effect mprF1 mutant does not affect in the synthesis of aminoacyl-PG in the laboratory condition. It also has no effect on susceptible to CAMPs, opsonic killing and autolysis. Therefore, it seems that mprF2 is the only functional mprF gene in E. faecalis in the laboratory condition. Unlike mprF found in other bacteria, mprF does not seem to be a major virulence factor in enterococci.CAEN-BU Sciences et STAPS (141182103) / SudocSudocFranceF
Uma análise das formas de remuneração dos sócios por meio do planejamento tributário
Activity and Interactions of Liposomal Antibiotics in Presence of Polyanions and Sputum of Patients with Cystic Fibrosis
BACKGROUND:To compare the effectiveness of liposomal tobramycin or polymyxin B against Pseudomonas aeruginosa in the Cystic Fibrosis (CF) sputum and its inhibition by common polyanionic components such as DNA, F-actin, lipopolysaccharides (LPS), and lipoteichoic acid (LTA). METHODOLOGY:Liposomal formulations were prepared from a mixture of 1,2-Dimyristoyl-sn-Glycero-3-Phosphocholine (DMPC) or 1,2-Dipalmitoyl-sn-Glycero-3-Phosphocholine (DPPC) and Cholesterol (Chol), respectively. Stability of the formulations in different biological milieus and antibacterial activities compared to conventional forms in the presence of the aforementioned inhibitory factors or CF sputum were evaluated. RESULTS:The formulations were stable in all conditions tested with no significant differences compared to the controls. Inhibition of antibiotic formulations by DNA/F-actin and LPS/LTA was concentration dependent. DNA/F-actin (125 to 1000 mg/L) and LPS/LTA (1 to 1000 mg/L) inhibited conventional tobramycin bioactivity, whereas, liposome-entrapped tobramycin was inhibited at higher concentrations--DNA/F-actin (500 to 1000 mg/L) and LPS/LTA (100 to 1000 mg/L). Neither polymyxin B formulation was inactivated by DNA/F-actin, but LPS/LTA (1 to 1000 mg/L) inhibited the drug in conventional form completely and higher concentrations of the inhibitors (100 to 1000 mg/L) was required to inhibit the liposome-entrapped polymyxin B. Co-incubation with inhibitory factors (1000 mg/L) increased conventional (16-fold) and liposomal (4-fold) tobramycin minimum bactericidal concentrations (MBCs), while both polymyxin B formulations were inhibited 64-fold. CONCLUSIONS:Liposome-entrapment reduced antibiotic inhibition up to 100-fold and the CFU of endogenous P. aeruginosa in sputum by 4-fold compared to the conventional antibiotic, suggesting their potential applications in CF lung infections
The Transcriptome of the Nosocomial Pathogen Enterococcus faecalis V583 Reveals Adaptive Responses to Growth in Blood
gains access to the bloodstream and establishes a persistent infection is not well understood.. infections
AATF/Che-1 acts as a phosphorylation-dependent molecular modulator to repress p53-driven apoptosis
Magnetic and Spectroscopic Studies on Copper(II) and Chromium(III) Complexes With Sulfur Chelating Ligands
Disorder effects in Mn12-acetate at 83 K
The structure of hexadeca-mu-acetato-tetraaquadodeca-mu(3) oxo-
dodecamanganese bis(acetic acid) tetrahydrate, [Mn12O12
(CH3COO)(16) (H2O)(4)].2CH(3)COOH.4H(2)O, known as Mn-12-
acetate, has been determined at 83 (2) K by X-ray diffraction
methods. The fourfold (S-4) molecular symmetry is disrupted by
a strong hydrogen-bonding interaction with the disordered
acetic acid molecule of solvation, which displaces one of the
acetate ligands in the cluster. Up to six Mn-12 isomers are
potentially present in the crystal lattice, which differ in the
number and arrangement of hydrogen-bonded acetic acid
molecules. These results considerably improve the structural
information available on this molecular nanomagnet, which was
first synthesized and characterized by Lis [Acta Cryst. (1980),
B36, 2042-2046]
Disorder effects in Mn12–acetate at 83 K
The structure of hexadeca-mu-acetato-tetraaquadodeca-mu3 oxo-dodecamanganese bis(acetic acid) tetrahydrate, [Mn12O12 (CH3COO)16(H2O)4].2CH3COOH.4H2O, known as Mn-12- acetate, has been determined at 83(2) K by X-ray diffraction methods. The fourfold (S-4) molecular symmetry is disrupted by a strong hydrogen-bonding interaction with the disordered acetic acid molecule of solvation, which displaces one of the acetate ligands in the cluster. Up to six Mn-12 isomers are potentially present in the crystal lattice, which differ in the number and arrangement of hydrogen-bonded acetic acid molecules. These results considerably improve the structural information available on this molecular nanomagnet, which was first synthesized and characterized by Lis [Acta Cryst. (1980), B36, 2042-2046]
Energy-barrier enhancement by ligand substitution in tetrairon(III) single-molecule magnets
A dramatic increase of the energy barrier (Ueff) in tetrairon(III) single-mol. magnets can be achieved by simple chem. modification. Site-specific replacement of the six methoxide bridges in [Fe4(OMe)6(dpm)6] (Hdpm = dipivaloylmethane; Ueff/kB = 3.5 K) with two tripodal 1,1,1-tris(hydroxymethyl)ethane (H3thme) ligands affords [Fe4(thme)2(dpm)6] with Ueff/kB = 15.6(2) K and a magnetic relaxation time exceeding 1000 s at T <0.2 K. The prepd. complex is trigonal, space group R-3c, Z = 6, R1 = 0.0370, R2 = 0.1089
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