[Mental health educational programs in schools: Experiences, needs and expectations expressed by students in France]. / L'éducation à la santé mentale à l'école : vécu, besoins et attentes exprimés par les étudiants en France.

AIMS: This study explores the experiences and expectations of young adults concerning mental health educational programs in schools. The scarcity of these programs leads us to deepen students' perspective in order to boost the establishment of such sessions. Indeed, this type of prevention plan can improve the access to care and reduce the impact of such disorders. METHODOLOGY: We have developed a standardized questionnaire to be filled online by students between the ages of 18 and 25 years, reached using Facebook pages of student associations of universities from different regions of France. RESULTS: From the 3rd to the 20th of July 2017, 1852 students filled in the questionnaire. In total, 1672 (90%) of the young adults had not experienced mental health educational programs in their school career. However, 1652 (90%) requested that these programs be a part of their academic career. The majority of the young adults (n=590, 56%) would have chosen a psychologist as leader for these programs, preferably (>80%) in a discussion around a difficult imaginary situation, using role-playing or a board game. Furthermore, 1067 (57%) young adults reported having felt the need to talk to someone about mental health during their school career. CONCLUSION: This exploratory study highlights the lack of mental health educational programs in schools and the need expressed by students themselves. It suggests directions to think about how to develop these mental health preventive programs, evoking their limits and advantages.

Purification and antigenic analysis of the major 25-kilodalton outer membrane protein of Brucella abortus.

The major 25-kDa outer membrane protein (Omp25) of Brucella abortus was purified and antigenically characterized by use of monoclonal antibodies (mAbs). Purification was achieved from the sodium dodecyl sulphate-insoluble (SDS-I) cell wall (CW) fraction of vaccine strain B. abortus B19 which was shown by use of mAbs to contain the two major outer membrane proteins of 25 and 36 kDa linked to peptidoglycan, smooth lipopolysaccharide (S-LPS), and rough LPS (R-LPS). Purity of Omp25 was checked with a number of mAbs directed to the different components of the SDS-I fraction. In ELISA, five anti-Omp25 mAbs, which showed significant binding to B. abortus whole cells and which are probably directed to conformational epitopes well-exposed on the bacterial surface, reacted poorly or not at all with the purified Omp25. Addition of R-LPS to purified Omp25 restored the binding capacity of these mAbs, which suggested that R-LPS may play an important role in reconstitution and exposure of conformational epitopes of Omp25. Immunoelectron microscopy showed that Omp25 was inserted into the R-LPS vesicles. Four of these anti-Omp25 mAbs probably recognize the same or closely located epitopes on Omp25, since one of the mAbs conjugated to peroxidase was inhibited in its binding in ELISA by the three others. Other anti-Omp25 mAbs showed strong binding to purified denatured Omp25 and their binding capacity was not affected by the addition of R-LPS to the purified Omp25. Thus, these results confirmed, as defined by the mAbs, the presence of both sequential and at least one conformational epitope on Omp25.

Growth phase-dependent variations in the outer membrane protein profile of Brucella melitensis.

Changes in Brucella cell envelope protein profiles were investigated with batch cultures of B. melitensis strain 16M in a 2-litre fermenter. Analysis of expression of outer membrane proteins (OMP) (apparent molecular masses of 10, 16.5, 19, 25-27, 31-34, 36-38 and 89 kDa) and heat-shock protein DnaK (73 kDa) was performed with monoclonal antibodies (mAb) and immunoblotting techniques. Synthesis of the 89-kDa OMP and the heat-shock protein DnaK was invariant during B. melitensis growth. Expression of the 10-, 19- and 36-38-kDa minor OMPs was never detected. Variations in profiles of some OMPs, i.e. 25-27-kDa and 31-34-kDa major proteins and 16.5-kDa minor protein, occurred during growth stages, principally at the end of the exponential growth phase. These variations consisted of shifts in apparent molecular masses for the 25-27-kDa and 31-34-kDa OMPs and of peptidoglycan association for the 16.5-kDa OMP. Therefore, whereas the strong association of major OMPs with peptidoglycan was confirmed, results suggested that the 16.5-kDa minor OMP is also a peptidoglycan-associated protein.

Antibody response to the 89-kDa outer membrane protein of Brucella in bovine brucellosis.

The antibody response of cattle to the minor 89-kDa outer-membrane protein (OMP) of brucella was measured by indirect ELISA with the purified protein and compared with the antibody response to smooth lipopolysaccharide (S-LPS). Pre-incubating sera with sonicated cell extracts of Escherichia coli prevented the binding of antibodies from uninfected animals to the 89-kDa OMP, suggesting the presence of one or more cross-reactive epitopes on this protein. In cattle infected experimentally with Brucella abortus, the antibody response to the 89-kDa OMP was later and less intense than that to S-LPS. In naturally infected cattle, 68% of animals showing an antibody response to S-LPS also showed an antibody response to the 89-kDa OMP. Results indicate that specific epitopes of the 89-kDa OMP in combination with those of other OMPs could be useful for diagnosis of brucellosis in cattle.

[Radiological evaluation of k-wire osteosynthesis, in comparison to fixed-angle-plate osteosynthesis, in patients aged 80 years or more with distal radius fractures]. / Radiologische Ergebnisse von K-Draht Osteosynthesen im Vergleich zu winkelstabilen Plattenosteosynthesen distaler Radiusfrakturen bei Patienten über 80 Lebensjahre.

BACKGROUND: This study evaluates the short-term radiological outcome of K-wire osteosynthesis (KWO) in comparison to the fixed-angle-plate osteosynthesis (ORIF) on distal radius fractures in elderly patients (aged 80 years or more) with osteoporotic bones. PATIENTS AND METHODS: This study retrospectivly compares the postoperative X-rays of distal radius fractures (obtained between the years of 1998-2009) of patients aged 80 years and above treated with KWO (228 fractures, mean age 85 years), with the results of patients who were treated with fixed-angle plate ORIF (120 fractures, mean age 84 years). Within the KWO results, we also further compared the radiological results of a static and a dynamic (Kapandji) KWO technique. Only patients with a postoperative, anatomic reduction, and those who were radiologically followed up in a period of 2 months and above were included. The radiological criteria included the palmar and radial inclination as well as the radial shortening. RESULTS: With KWO performed in a static technique, 24% of the postoperative results showed no reduction loss. The use of the dynamic Kapandji technique KWO, improved the positive results to 63%. However, almost a third of the fractures (30%) treated with KWO, had shifted back to their preoperative positions, or worsened overall. The fixed angle plate (ORIF) was able to maintain 76% of all fractures in their postoperative positions. Merely 1.7% of the ORIF group sustained a complete reduction loss. The fixed-angle plate osteosynthesis shows a significant decrease of cases in which a complete repositioning loss is experienced. CONCLUSION: Although the importance of anatomic reconstruction of distal radius fractures is often debated in cases involving elderly patients, it is our considered opinion that, should an operative solution be chosen, one should consider the fixed-angle-plate osteosynthesis as the preferred operation method to prevent loss of reduction.

Isolation of three Brucella abortus cell-wall antigens protective in murine experimental brucellosis.

The insoluble fraction, SDS-I, obtained by boiling cell-walls of Brucella abortus in sodium dodecyl sulfate (SDS) was hydrolyzed by lysozyme. Three major bands of apparent molecular weight 37000 (I), 25000 (II), 15000 (III) were isolated by gel slicing after polyacrylamide gel electrophoresis in the presence of SDS. The three bands were injected subcutaneously to mice using Freund incomplete adjuvant and immunity was tested one month later by intraperitoneal administration of a virulent strain of B. abortus. Fifteen days after challenge, numbers of viable brucella within the spleens were determined. The isolated bands, I, II and III were able to protect mice at a level corresponding to the killed whole-cells Brucella melitensis H38 reference vaccine.

Enzyme-linked immunosorbent assay with partially purified cytosoluble 28-kilodalton protein for serological differentiation between Brucella melitensis-infected and B. melitensis Rev.1-vaccinated sheep.

The problem of differentiating sheep infected with Brucella melitensis from those vaccinated or exposed to cross-reaching organisms has not been resolved by conventional serological tests or through the use of the smooth lipopolysaccharide in primary binding assays. We therefore analyzed sera from ewes experimentally infected with B. melitensis H38, from ewes naturally infected with B. melitensis, and from B. melitensis Rev.1-vaccinated ewes by enzyme-linked immunosorbent assay with three antigenic fractions: O polysaccharide, a cytosoluble protein extract (CPE) from the rough strain B. melitensis B115, and a partially purified cytosoluble protein of 28 kDa (CP28) from the CPE. Immunoglobulin G anti-O polysaccharide and anti-CPE responses were detected in all groups of animals tested (Rev.1 vaccinated and B. melitensis infected). However, false-positive reactions with CPE occurred with sera from Brucella-free ewes. The use of partially purified CP28 abolished these false-positive reactions. Furthermore, no immunoglobulin G antibodies against CP28 were detected in sera from vaccinated ewes, whereas 80% (8 of 10) of ewes experimentally infected with B. melitensis H38 and 89% (25 of 28) of naturally infected ewes showed various degrees of anti-CP28 reactivity (absorbance values of between 0.5 and 2.5). The results obtained with CP28 showed the potential usefulness of this antigen to permit the detection of B. melitensis-infected ewes and their differentiation from B. melitensis Rev.1-vaccinated ones.

Mapping and identification of Brucella melitensis proteins by two-dimensional electrophoresis and microsequencing.

Two-dimensional (2-D) gel electrophoresis was used to map Brucella melitensis proteins. The 2-D proteins map of B. melitensis B115 revealed 595 silver-stained protein spots separated by both isoelectric point and molecular mass. Twenty-five proteins were identified either by immunoblotting using monoclonal antibodies (MAbs) or by N-terminal microsequencing. The protein spots identified by MAbs were the 89 kDa outer membrane protein, DnaK, bacterioferritin, CP24, and BP26. Some spots were identified by N-terminal microsequencing as proteins whose sequences had been reported previously from Brucella, such as three heat-shock proteins, namely DnaK, GroEL and GroES; bacterioferritin; Cu-Zn superoxide dismutase; and the 50S ribosomal protein L7/L12. Other proteins had amino acid sequences homologous with those of various proteins from other bacteria found in protein databases: ClpP; the 10K-S protein; the ORFU phosphoprotein; succinyl-CoA synthetase alpha sub-unit; an inorganic pyrophosphatase; the Fe and/or Mn superoxide dismutase; the nucleoside diphosphate kinase, an amino acid ABC type transporter, and an electron transfer flavoprotein small subunit. Seven proteins were identified with N-terminal sequences not yet reported in databases. The 2-D map established in this study will be the basis for comparative studies of protein expression in Brucella.

Identification and characterization of Brucella ovis immunogenic proteins using two-dimensional electrophoresis and immunoblotting.

In a previous report, proteins from Brucella melitensis were characterized by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) and N-terminal microsequencing. In the present report, we have extended this study to the second etiologic agent in ovine brucellosis, B. ovis, responsible for ram epididymitis and infertility. The combination of 2-D gel electrophoresis and protein microsequencing facilitated the location and identification of the major proteins of B. ovis on the 2-D pattern. These proteins comprised cytoplasmic, periplasmic, and some membrane proteins except the major outer membrane proteins. By comparing 2-D gel profiles of B. ovis with that of B. melitensis described previously, a few proteins with different expression levels were readily identified. Serum from a ram naturally infected with B. ovis was used in immunoblotting studies to identify immunogenic proteins recognized during the course of infection. This serum showed antibody reactivity against approximately 82 protein spots. Twenty-one of these proteins were identified either by use of monoclonal antibodies or by N-terminal microsequencing. Several proteins previously described in earlier Brucella works were identified: the 89 kDa outer membrane protein, DnaK, GroEL, BP26, and Cu-Zn superoxide dismutase. Eight proteins had amino acid sequences homologous to those of various proteins from other bacteria found in protein databases; NikA, dihydrolipoamide succinyltransferase, a hypothetical 31 kDa protein, malate dehydrogenase, succinyl-CoA synthetase alpha subunit, an amino acid ABC type transporter, Leu/Ile/Val-binding protein precursor, and ClpP. The remaining eight proteins had N-terminal sequences lacking similarity to existing databases entries. Thus, the 2-D PAGE analysis provided a convenient first approach in the characterization of immunogenic proteins.