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Titre : | Mécanismes de résistance aux aminoglycosides : le rôle du polyphosphate |
Auteurs : | Mostafa Shehrzad, Auteur ; François Beaufay, Promoteur |
Type de document : | Travail de fin d'études |
Editeur : | Woluwe-Saint-Lambert : Haute École Léonard de Vinci, 2022 |
Langues: | Français |
Index. décimale : | TFE - Biologie médicale |
Mots-clés: | Polyphosphate ; sous-unités ribosomiques ; aminogmycosides |
Résumé : |
Comprendre le rôle du polyphosphate dans la résistance aux aminoglycosides et le rôle potentiel du polyP dans la traduction.
The development of antibiotics in the middle of the 20th century revolutionized modern medicine and was a large contributor on the doubling of human life expectancy in the 20th century. However, misuse led to the rapid spread of antibiotic resistance to the point of being, today, a major public health problem. There is now an urge to re-evaluate how we use antibiotics and to find new ways to treat infection disease. Polyphosphate (PolyP), a ubiquitous polymer of inorganic phosphate, is one of these new potential targets for drug development as it is at the center of the stress response in bacteria. Dr. François Beaufay also observed that the absence of polyphosphate sensitizes bacteria against aminoglycosides, a class of antibiotic targeting translation. The aim of this work is to identify the role of polyphosphate in protein synthesis related to resistance to aminoglycosides. Firstly, we studied the role of PolyP in the stress responses by E. coli caused by aminoglycoside, mainly streptomycin. Using an overexpression library, we looked for sequence able to rescue the defect observed in presence of streptomycin of an E. coli unable to produce to polyP. Then, we quantified the effect of PolyP on translational fidelity using a modified version of the well-described Beta-galactosidase assay. Interestingly, high levels of polyP led to an increased in fidelity during proteins synthesis. These observations are in accordance with results obtained by previous studying showing that the absence of polyP led to a decrease in fidelity. We also hope find the sequence able to rescue the defect of PolyP in presence of streptomycin, after having identified the result of our library. |
Accès : | Identifiez-vous avant d'accéder au document électronique |
Disponible en ligne : | Oui |
Lieu du stage : | GOSSELIES, Charleroi, Rue des Professeurs Jeener & Brachet, 12 |
Département : | Biologie médicale |
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TFE - Biologie médicale Adobe Acrobat PDF |