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Subproteomic signature comparison of in vitro selected fluoroquinolone resistance and ciprofloxacin stress in Salmonella Typhimurium DT104B |
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| Authors: | Susana Correia Michel Hébraud Ingrid Chafsey Christophe Chambon Didier Viala Carmen Torres |
| Institution: | 1. Functional Genomics and Proteomics Unit, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal;2. Department of Genetics and Biotechnology, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal;3. Veterinary Science Department, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal;4. UCIBIO-REQUIMTE, Faculty of Science and Technology, Nova University of Lisbon, Caparica, Portugal;5. UR454 Microbiology, Institut National de la Recherche Agronomique (INRA), Centre Auvergne-Rh?ne-Alpes, site de Theix, Saint-Genès Champanelle, France;6. Plate-Forme d’Exploration du Métabolisme composante protéomique, UR370 QuaPA, Institut National de la Recherche Agronomique (INRA), Centre Auvergne-Rh?ne-Alpes, site de Theix, Saint-Genès Champanelle, France;7. Plate-Forme d’Exploration du Métabolisme composante protéomique, UR370 QuaPA, Institut National de la Recherche Agronomique (INRA), Centre Auvergne-Rh?ne-Alpes, site de Theix, Saint-Genès Champanelle, France;8. área de Bioquímica y Biología Molecular, Universidad de La Rioja, Logro?o, Spain |
| Abstract: | Background: Fluoroquinolone resistance in nontyphoidal Salmonella is a situation of serious and international concern, particularly in S. Typhimurium DT104B multiresistant strains. Although known to be multifactorial, fluoroquinolone resistance is still far from a complete understanding. Methods: Subproteome changes between an experimentally selected fluoroquinolone-resistant strain (Se6-M) and its parent strain (Se6), and also in Se6-M under ciprofloxacin (CIP) stress, were evaluated in order to give new insights into the mechanisms involved. Proteomes were compared at the intracellular and membrane levels by a 2-DE~LC-MS/MS and a shotgun LC-MS/MS approach, respectively. Results: In total, 35 differentially abundant proteins were identified when comparing Se6 with Se6-M (25 more abundant in Se6 and 10 more abundant in Se6-M) and 82 were identified between Se6-M and Se6-M+CIP (51 more abundant in Se6-M and 31 more abundant under ciprofloxacin stress). Conclusion: Several proteins with known and possible roles in quinolone resistance were identified which provide important information about mechanism-related differential protein expression, supporting the current knowledge and also leading to new testable hypotheses on the mechanism of action of fluoroquinolone drugs. |
| Keywords: | Antimicrobial resistance comparative subproteomics LC-MS/MS Salmonella Typhimurium DT104B shotgun proteomics 2-DE |