Biomedical subjects

N Chevalier

Publications and source records attributed to N Chevalier.

At least 109 records · Page 6Linked to original sources

PubMed2002

Measurement of the B0-B-0 oscillation frequency with inclusive dilepton events.

The B0-B-0 oscillation frequency has been measured with a sample of 23 x 10(6) BB- pairs collected with the BABAR detector at the PEP-II asymmetric B Factory at SLAC. In this sample, we select events in which both B mesons decay semileptonically and use the charge of the leptons to identify the flavor of each B meson. A simultaneous fit to the decay time difference distributions for opposite- and same-sign dilepton events gives deltamd = 0.493+/-0.012(stat)+/-0.009(syst) ps-1.

Journal Article↗

PubMed2002

Search for T and CP violation in B0-B-0 mixing with inclusive dilepton events.

We report the results of a search for T and CP violation in B0-B-0 mixing using an inclusive dilepton sample collected by the BABAR experiment at the PEP-II B Factory. The asymmetry between l+l+ and l-l- events allows us to compare the probabilities for B-0-->B0 and B0-->B-0 oscillations and thus probe T and CP invariance. Using a sample of 23 x 10(6) BB- pairs, we measure a same-sign dilepton asymmetry of A(T/CP) = [0.5+/-1.2(stat)+/-1.4(syst)]%. For the modulus of the ratio of complex mixing parameters p and q, we obtain q/p = 0.998+/-0.006(stat)+/-0.007(syst).

Journal Article↗

PubMed2002

Measurement of B --> K*gamma branching fractions and charge asymmetries.

The branching fractions of the exclusive decays B0-->K(*0)gamma and B+-->K(*+)gamma are measured from a sample of (22.74+/-0.36)x10(6) BB decays collected with the BABAR detector at the PEP-II asymmetric e(+)e(-) collider. We find B (B0-->K(*0)gamma) = [4.23+/-0.40(stat)+/-0.22(syst)]x10(-5), B(B+-->K(*+)gamma) = [3.83+/-0.62(stat)+/-0.22(syst)]x10(-5) and constrain the CP-violating charge asymmetry to be -0.170 K(*)gamma)<0.082 at 90% C.L.

Journal Article↗

PubMed2002

[Peri-hepatitis abscess secondary to pelvic peritonitis].

OBJECTIVE: To report the case of a 42-year-old patient referred for exploration of a tumor of the right flank and evidence of inflammation. MATERIAL: and methods. Ultrasonography and computed tomography showed a liver mass associated with a heterogeneous adnexal mass. Serum CA-125 was elevated and ovarian cancer with liver metastasis was suspected. An alternative diagnosis was salpingitis complicated by Fitz-Hugh-Curtis syndrome in this patient wearing an intra-uterine contraceptive device. RESULTS: Exploratory laparoscopy was performed and confirmed the diagnosis of salpingitis complicated by an ovarian abscess and Fitz-Hugh-Curtis syndrome with rare abscess formation. Outcome was favorable after adapted antibiotic treatment. CONCLUSION: Fitz-Hugh-Curtis syndrome can take on an atypical aspect and should be entertained as a possible diagnosis in young women presenting pain of the right flank and fever.

Acute Disease↗

PubMed2001

Search for the decay B0-->gammagamma.

We present a limit on the branching fraction for the decay B0-->gammagamma using data collected at the Upsilon(4S) resonance with the BABAR detector at the PEP-II asymmetric energy e+e- collider. Based on the observation of one event in the signal region, out of a sample of 21.3x10(6) e+e--->Upsilon(4S)-->BB decays, we establish an upper limit on the branching fraction of B(B0-->gammagamma)<1.7x10(-6) at the 90% confidence level. This result substantially improves upon existing limits.

Journal Article↗

PubMed2001

Measurement of the B--> J/psiK*(892) decay amplitudes.

We present a measurement of the decay amplitudes in B-->J/psiK*(892) channels using 20.7 fb(-1) of data collected at the Upsilon(4S) resonance with the BABAR detector at PEP-II. We measure a P-wave fraction R(perpendicular) = (16.0 +/- 3.2 +/- 1.4)% and a longitudinal polarization fraction (59.7 +/- 2.8 +/- 2.4)%. The measurement of a relative phase that is neither 0 nor pi, phi = 2.50 +/- 0.20 +/-0.08 radians, favors a departure from the factorization hypothesis. Although the decay B-->/psiK(pi) proceeds mainly via K*(892), there is also evidence for K2*(1430) and K(pi) S-wave contributions.

Journal Article↗

PubMed2001

Measurements of the branching fractions of exclusive charmless B meson decays with eta(') or omega mesons.

We present the results of searches for B decays to charmless two-body final states containing eta(') or omega mesons, based on 20.7 fb(-1) of data collected with the BABAR detector. We find the branching fractions Beta(B(+)-->eta(')K(+)) = (70+/-8+/-5) x 10(-6), Beta(B(0)-->eta(')K(0)) = (42(+13)(-11) +/- 4) x 10(-6), and Beta(B(+)-->omega pi(+)) = (6.6(+2.1)(-1.8) +/- 0.7) x 10(-6), where the first error quoted is statistical and the second is systematic. We give measurements of four additional modes for which the 90% confidence level upper limits are Beta(B(+)-->eta(')pi(+)) < 12 x 10(-6), Beta(B(+)-->omega K(+)) < 4 x 10(-6), Beta(B(0)-->omega K(0)) < 13 x 10(-6), and Beta(B(0)-->omega pi(0)) < 3 x 10(-6).

Journal Article↗

PubMed2001

Measurement of the B(0) and B(+) meson lifetimes with fully reconstructed hadronic final states.

The B(0) and B(+) meson lifetimes have been measured in e(+)e(-) annihilation data collected in 1999 and 2000 with the BABAR detector at center-of-mass energies near the Upsilon(4S) resonance. Events are selected in which one B meson is fully reconstructed in a hadronic final state while the second B meson is reconstructed inclusively. A combined fit to the B(0) and the B(+) decay time difference distributions yields tau(B(0)) = 1.546+/-0.032(stat)+/-0.022(syst) ps, tau(B(+)) = 1.673+/-0.032(stat)+/-0.023(syst) ps, and tau(B(+))/tau(B(0)) = 1.082+/-0.026(stat)+/-0.012(syst).

Journal Article↗

PubMed2001

Measurement of J/psi production in continuum e(+)e(-) annihilations near square root of s = 10.6 GeV.

The production of J/psi mesons in continuum e(+)e(-) annihilations has been studied with the BABAR detector at energies near the Upsilon(4S) resonance. The mesons are distinguished from J/psi production in B decays through their center-of-mass momentum and energy. We measure the cross section e(+)e(-)-->J/psi X to be 2.52+/-0.21+/-0.21 pb. We set a 90% C.L. upper limit on the branching fraction for direct Upsilon(4S)-->J/psi X decays at 4.7 x 10(-4).

Journal Article↗

PubMed2001

Measurement of branching fractions and search for CP-violating charge asymmetries in charmless two-body B decays into pions and kaons.

We present measurements, based on a sample of approximately 23x10(6) BB pairs, of the branching fractions and a search for CP-violating charge asymmetries in charmless hadronic decays of B mesons into two-body final states of kaons and pions. We find the branching fractions B(B0-->pi(+)pi(-)) = (4.1+/-1.0+/-0.7)x10(-6), B(B0-->K+pi(-)) = (16.7+/-1.6+/-1.3)x10(-6), B(B+-->K+pi(0)) = (10.8(+2.1)(-1.9)+/-1.0)x10(-6), B(B+-->K0pi(+)) = (18.2(+3.3)(-3.0)+/-2.0)x10(-6), B(B0-->K0pi(0)) = (8.2(+3.1)(-2.7)+/-1.2)x10(-6). We also report 90% confidence level upper limits for B meson decays to the pi(+)pi(0), K+K-, and K0K+ final states. In addition, charge asymmetries have been found to be consistent with zero, where the statistical precision is in the range of +/-0.10 to +/-0.18, depending on the decay mode.

Journal Article↗

PubMed2001

Measurement of the decays B--> phiK and B--> phiK*.

We have observed the decays B--> phiK and phiK(*) in a sample of over 45 million B mesons collected with the BABAR detector at the PEP-II collider. The measured branching fractions are B(B+--> phiK+) = (7.7(+1.6)(-1.4)+/-0.8)x10(-6), B(B0--> phiK0) = (8.1(+3.1)(-2.5)+/-0.8)x10(-6), B(B+--> phiK(*+)) = (9.7(+4.2)(-3.4)+/-1.7)x10(-6), and B(B0--> phiK(*0)) = (8.7(+2.5)(-2.1)+/-1.1)x10(-6). We also report the upper limit B(B+--> phipi(+))<1.4x10(-6) ( 90% C.L.).

Journal Article↗

PubMed2001

Observation of CP violation in the B(0) meson system.

We present an updated measurement of time-dependent CP-violating asymmetries in neutral B decays with the BABAR detector at the PEP-II asymmetric B Factory at SLAC. This result uses an additional sample of Upsilon(4S) decays collected in 2001, bringing the data available to 32 x 10(6) BB macro pairs. We select events in which one neutral B meson is fully reconstructed in a final state containing charmonium and the flavor of the other neutral B meson is determined from its decay products. The amplitude of the CP-violating asymmetry, which in the standard model is proportional to sin2 beta, is derived from the decay time distributions in such events. The result sin2 beta = 0.59+/-0.14(stat)+/-0.05(syst) establishes CP violation in the B(0) meson system. We also determine absolute value of lambda = 0.93+/-0.09(stat)+/-0.03(syst), consistent with no direct CP violation.

Journal Article↗

PubMed2001

The expression and intracellular distribution of phosphoglycerate kinase isoenzymes in Trypanosoma cruzi.

In this paper, we report the subcellular distribution of phosphoglycerate kinase (PGK) in epimastigotes of Trypanosoma cruzi. Approximately 80% of the PGK activity was found in the cytosol, 20% in the glycosomes. Western blot analysis suggested that two isoenzymes of 56 and 48 kDa, respectively, are responsible for the glycosomal PGK activity, whereas the cytosolic activity should be attributed to a single PGK of 48 kDa. In analogy to the situation previously reported for PGK in Trypanosoma brucei, these isoenzymes were called PGKA, C and B, respectively. However, in T. cruzi, PGKA seems not to be a minor enzyme like its counterpart in T. brucei. Whereas PGKC behaved as a soluble glycosomal matrix protein, PGKA appeared to be present at the inner surface of the organelle's membrane. After alkaline carbonate treatment, the enzyme remained associated with the particulate fraction of the organelles. Upon solubilization of glycosomes with Triton X-114, PGKA was recovered from the detergent phase, indicating its (partial) hydrophobic character and therefore, a possible hydrophobic interaction with the membrane. The PGKA gene was cloned and sequenced, but the predicted amino-acid sequence did not reveal an obvious clue as to the mechanism by which the enzyme is attached to the glycosomal membrane.

Amino Acid Sequence↗

PubMed2000

Trypanosoma brucei contains a 2,3-bisphosphoglycerate independent phosphoglycerate mutase.

Assays of phosphoglycerate mutase (PGAM) activity in lysates of bloodstream form Trypanosoma brucei appeared not to require exogenous 2,3-bisphosphoglycerate, thus suggesting that this protist contains an enzyme belonging to the class of cofactor-independent PGAMs. A gene encoding a polypeptide with motifs characteristic for this class of enzymes was cloned. The predicted T. brucei PGAM polypeptide contains 549 amino acids, with Mr 60 557 and pI 5.5. Comparison with 15 cofactor-independent PGAM sequences available in databases showed that the amino-acid sequence of the trypanosome enzyme has 59-62% identity with plant PGAMs and 29-35% with eubacterial enzymes. A low 28% identity was observed with the only available invertebrate sequence. The trypanosome enzyme has been expressed in Escherichia coli, purified to homogeneity and subjected to preliminary kinetic analysis. Previous studies have shown that cofactor-dependent and -independent PGAMs are not homologous. It has been inferred that the cofactor-independent PGAMs are in fact homologous to a family of metalloenzymes containing alkaline phosphatases and sulphatases. Prediction of the secondary structure of T. brucei PGAM and threading the sequence into the known crystal structure of E. coli alkaline phosphatase (AP) confirmed this homology, despite the very low sequence identity. Generally, a good match between predicted (PGAM) and actual (AP) secondary structure elements was observed. In contrast to trypanosomes, glycolysis in all vertebrates involves a cofactor-dependent PGAM. The presence of distinct nonhomologous PGAMs in the parasite and its human host offers great potential for the design of selective inhibitors which could form leads for new trypanocidal drugs.

2,3-Diphosphoglycerate↗

PubMed1998

Purification and characterisation of the phosphoglycerate kinase isoenzymes of Trypanosoma brucei expressed in Escherichia coli.

The Trypanosoma brucei phosphoglycerate kinase (PGK) glycosomal and cytosolic isoenzymes have been overexpressed in Escherichia coli and purified to near-homogeneity. Both enzymes were similar to the corresponding natural proteins with respect to their physicochemical and kinetic properties. In addition, a mutant of the glycosomal PGK lacking the 20 amino acid long C-terminal extension was overexpressed and purified. Various properties of this truncated glycosomal PGK were examined and it was found that in some aspects the protein behaved quite differently when compared with its natural counterpart. This was notably the case for the apparent Km for 3-phosphoglyceric acid, its sensitivity to inhibitors and its response to salts and guanidine HCl. However, its Vmax was found to be similar to that of the natural glycosomal PGK. These results suggest that the changes in the C-terminus caused a conformational change effecting the 3-phosphoglyceric acid binding site located at the N-terminal domain of the protein.

Animals↗

PubMed1998

Pyruvate kinase of Trypanosoma brucei: overexpression, purification, and functional characterization of wild-type and mutated enzyme.

A procedure was developed for overexpression of Trypanosoma brucei pyruvate kinase in Escherichia coli. The enzyme was purified to near-homogeneity from the bacterial lysate by first removing nucleic acids and contaminating proteins by protamine sulfate precipitation and subsequent passage over a phosphocellulose column. The purified protein is essentially indistinguishable in its physicochemical and kinetic properties from the enzyme purified from trypanosomes. Furthermore, experiments were undertaken to locate the binding site of the allosteric effector fructose 2,6-bisphosphate. Regulation of pyruvate kinase by this effector is unique to trypanosomes and related protozoan organisms. Therefore, a three-dimensional structure model of the enzyme was made, and a putative effector-binding site could be identified in an interdomain cleft. Four residues in this cleft were mutated, and the mutant proteins were produced and purified, using the same methodology as for the wild-type pyruvate kinase. Some mutants showed only minor changes in the activation by the effector. However, substitution of Arg22 by Gly resulted in a 9.2-fold higher S(0.5) for phosphoenolpyruvate and a significantly smaller kcat than the wild-type enzyme. Furthermore, the apparent affinity of this mutant for the allosteric effectors fructose 1,6-bisphosphate and fructose 2,6-bisphosphate was 8.2- and 5.2-fold lower than that of its wild-type counterpart. Effector binding was also affected, although to a lesser extent, in a mutant Phe463Val. These data indicate that particularly residue Arg22, but also Phe463, are somehow involved in the binding of the allosteric effectors.

Animals↗

PubMed1997

The glycosomal ATP-dependent phosphofructokinase of Trypanosoma brucei must have evolved from an ancestral pyrophosphate-dependent enzyme.

Trypanosoma brucei contains an ATP-dependent phosphofructokinase (PFK), located in its glycosomes, which are peroxisome-like organelles sequestering the majority of its glycolytic enzymes. In this paper, we report the cloning and sequencing of the single-copy gene encoding this enzyme. Its amino-acid sequence is more similar to pyrophosphate (PPi)-dependent PFKs than to other ATP-dependent PFKs. A phylogenetic analysis suggests that the enzyme must have been derived from a PPi-dependent ancestral PFK, which changed its phospho-donor specificity during evolution. The enzyme is no longer capable of using PPi as phospho substrate, nor can it catalyze the reverse reaction as PPi-PFKs generally can. Moreover, the presence of a high pyrophosphatase activity in the cell renders it unlikely that PPi can function as free-energy source in present-day trypanosomes. It remains to be determined which mutations were responsible for the change in phospho-substrate specificity of the trypanosomatid PFK. As a result of its particular evolutionary history, the T. brucei PFK shows many structural differences, even at the active site, when compared with other ATP-dependent PFKs. These differences offer great potential for the structure-based design of trypanocidal drugs.

Adenosine Triphosphate↗

PubMed1995

High-level expression of Trypanosoma brucei fructose-1,6-bisphosphate aldolase in Escherichia coli and purification of the enzyme.

A procedure has been developed for high-level expression of Trypanosoma brucei fructose-bisphosphate aldolase in Escherichia coli. Therefore, a specific restriction site was introduced by mutagenesis at the front of the gene, enabling its ligation in an expression plasmid, immediately downstream of the regulatory sequences. Growth conditions were established for production of high amounts of soluble and active enzyme. Aldolase was purified to near-homogeneity from the soluble fraction of the bacterial lysate by nuclease treatment, differential precipitation steps, and passage over a CM-Sepharose column. From a 1-liter culture of E. coli cells, 60-120 mg of purified protein that is essentially indistinguishable in physicochemical and kinetic properties and in stability from the enzyme purified from trypanosomes grown in infected laboratory animals was reproducibly obtained.

Animals↗