Les activités de mouvement dans les classes de 1-2H

Ce travail de recherche se base sur les activités de mouvement présentes dans les classes de 1-2H. Il vise à comprendre les conceptions du mouvement qu’ont les enseignants de ces degrés, expliciter les différentes pratiques qu’ils mettent en place ainsi qu’à mettre en lumière les obstacles qui peuvent surgir. Afin de mieux comprendre ce vaste sujet, ma problématique aborde d’abord le développement de l’enfant ainsi que la place et l’évolution du mouvement au sein de la classe. Ensuite, je présente les différents programmes déjà en place dans certaines classes favorisant le mouvement pour finalement réaliser une analyse du plan d’études romand, ceci afin d’observer la place du mouvement dans les différentes disciplines. Par le biais de six entretiens semi-directifs, je récolte des données auprès de deux groupes d’enseignants : ceux qui entrent dans la profession et ceux qui sont déjà experts. Les données récoltées me permettent d’effectuer une analyse qualitative et de comparer les différentes réponses pour en tirer des constats. De plus, ceux-ci sont comparés en fonction des deux groupes d’enseignants choisis. Au terme de mon analyse, je constate que les enseignants experts cherchent à collaborer pour améliorer leurs connaissances et leurs pratiques en lien avec le mouvement en classe, alors que les enseignants qui entrent dans la profession cherchent des outils « clé en main », des idées à mettre rapidement en place

Identification of the neutralizing epitopes of Merkel cell polyomavirus major capsid protein within the BC and EF surface loops.

Merkel cell polyomavirus (MCPyV) is the first polyomavirus clearly associated with a human cancer, i.e. the Merkel cell carcinoma (MCC). Polyomaviruses are small naked DNA viruses that induce a robust polyclonal antibody response against the major capsid protein (VP1). However, the polyomavirus VP1 capsid protein epitopes have not been identified to date. The aim of this study was to identify the neutralizing epitopes of the MCPyV capsid. For this goal, four VP1 mutants were generated by insertional mutagenesis in the BC, DE, EF and HI loops between amino acids 88-89, 150-151, 189-190, and 296-297, respectively. The reactivity of these mutants and wild-type VLPs was then investigated with anti-VP1 monoclonal antibodies and anti-MCPyV positive human sera. The findings together suggest that immunodominant conformational neutralizing epitopes are present at the surface of the MCPyV VLPs and are clustered within BC and EF loops

High levels of antibodies against merkel cell polyomavirus identify a subset of patients with merkel cell carcinoma with better clinical outcome.

PURPOSE: A new human polyomavirus, Merkel cell polyomavirus (MCV), was identified in 2008 in tumor tissue of patients with Merkel cell carcinoma (MCC), a relatively rare human skin cancer. In this study, we investigated patients with MCC and controls for the presence of antibodies against MCV and their association with clinical characteristics. PATIENTS AND METHODS: Antibodies against MCV were investigated by enzyme-linked immunosorbent assay in 68 patients with MCC and 82 controls using VP1 virus-like particles produced in insect cells. RESULTS: Antibodies against MCV were detected in all patients with MCC and in 85% of controls. However, high antibody titers (> 10,000) were rarely observed in controls (7.3%) and they were detected in 64.7% of patients with MCC (P < .001) in contrast to the absence of VP1 expression in tumor samples. In addition, the geometric mean titer of anti-MCV in patients with MCC was around 14 times higher than that observed in MCV-positive controls (P < .001) and was not correlated with tumor viral load. High antibody titers were not found to be associated with any subject or tumor characteristics, but better progression-free survival was observed in patients with high antibody titers (hazard ratio, 4.6; 95% CI, 1.7 to 12.2; P = .002). CONCLUSION: High titers of MCV antibodies in a much higher proportion of patients with MCC than in controls confirmed the association between MCV infection and MCC. The findings also indicated that a better progression-free survival occurred in patients with high MCV antibody titers and suggested that there are at least two distinct etiologic causes of MCC

High levels of antibodies against merkel cell polyomavirus identify a subset of patients with merkel cell carcinoma with better clinical outcome.

International audiencePURPOSE: A new human polyomavirus, Merkel cell polyomavirus (MCV), was identified in 2008 in tumor tissue of patients with Merkel cell carcinoma (MCC), a relatively rare human skin cancer. In this study, we investigated patients with MCC and controls for the presence of antibodies against MCV and their association with clinical characteristics. PATIENTS AND METHODS: Antibodies against MCV were investigated by enzyme-linked immunosorbent assay in 68 patients with MCC and 82 controls using VP1 virus-like particles produced in insect cells. RESULTS: Antibodies against MCV were detected in all patients with MCC and in 85% of controls. However, high antibody titers (> 10,000) were rarely observed in controls (7.3%) and they were detected in 64.7% of patients with MCC (P < .001) in contrast to the absence of VP1 expression in tumor samples. In addition, the geometric mean titer of anti-MCV in patients with MCC was around 14 times higher than that observed in MCV-positive controls (P < .001) and was not correlated with tumor viral load. High antibody titers were not found to be associated with any subject or tumor characteristics, but better progression-free survival was observed in patients with high antibody titers (hazard ratio, 4.6; 95% CI, 1.7 to 12.2; P = .002). CONCLUSION: High titers of MCV antibodies in a much higher proportion of patients with MCC than in controls confirmed the association between MCV infection and MCC. The findings also indicated that a better progression-free survival occurred in patients with high MCV antibody titers and suggested that there are at least two distinct etiologic causes of MCC

Monoclonal antibodies neutralization mechanism after pre (black) or post (white) MCPyV pseudovirions attachment.

<p>For the detection of neutralizing antibodies, COS-7 cells (10⁴/well) and MCPyV luciferase pseudovirions (0.2 RLU) were used. For the pre attachment determination, pseudovirions were mixed with monoclonal antibodies supernatants diluted 1:3 during 1 h and then added to the cells for 3 h at 37°C. The mixture was removed and 100 μl of DMEM-FCS were added. For investigation of post-attachment neutralization, pseudovirions were bound to cells for 1 h at 4°C. Unbound virions were removed and then antibodies diluted 1:3 were added during 1h. The antibodies were removed and 100 μl of DMEM-FCS were added. After incubation for 48 h at 37°C the luciferase activity was measure. The results were expressed as the percentage of inhibition of luciferase activity. The data presented are the means of three determinations performed in duplicate (+/- SEM).</p

ELISA reactivity of 10 neutralizing anti-MCPyV positive human sera (MCC patients) against MCPyV insertional mutants BC, DE, EF and HI.

<p>In order to characterize the epitopes of the MCPyV VP1, the reactivity of the human sera was analyzed from ten patients using the MCPyV wt VP1 VLPs and the four mutants with insertion within the BC, DE, EF and HI VP1 loops. ELISAs were performed using neutralizing anti-MCPyV positive human sera diluted 1:1000. The results are presented as relative binding defined as the reactivity of human serum to mutant VLPs divided by the reactivity of the same human serum observed with wild-type VLPs. The data presented are the means of three determinations (+/- SEM).</p

ELISA reactivity of MCPyV monoclonal antibodies against MCPyV insertional mutants BC, DE, EF and HI.

<p>In order to characterize the epitopes of the MCPyV VP1, the reactivity of mAbs was analyzed using the MCPyV wt VP1 VLPs and the four mutants with insertion within the BC, DE, EF and HI VP1 loops. ELISAs were performed using hybridoma culture supernatants diluted 1:3. The results are presented as relative binding defined as the reactivity of mAb to mutant VLPs divided by the reactivity of the same mAb observed with wild-type VLPs. The data presented are the means of three determinations (+/- SEM).</p