Subproteomic signature comparison of in vitro selected fluoroquinolone resistance and ciprofloxacin stress in Salmonella Typhimurium DT104B
- Correia, S. 2227
- Hébraud, M. 46
- Chafsey, I. 4
- Chambon, C. 6
- Viala, D. 6
- Torres, C. 1
- Caniça, M. 5
- Capelo, J.L. 47
- Poeta, P. 27
- Igrejas, G. 222
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1
Universidad de La Rioja
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2
Universidade de Trás-os-Montes e Alto Douro
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- 3 Faculty of Sciences and Technology, ProteoMass Scientific Society, Caparica, Portugal
- 4 Institut National de la Recherche Agronomique (INRA), Centre Auvergne-Rhône-Alpes, UR454 Microbiology, site de Theix, Saint-Genès Champanelle, France
- 5 National Reference Laboratory of Antibiotic Resistances and Healthcare Associated Infections (NRL-AMR-HAI), Department of Infectious Diseases, National Health Institute Doutor Ricardo Jorge (INSA), Lisbon, Portugal
- 6 Plate-Forme d’Exploration du Métabolisme composante protéomique, UR370 QuaPA, Institut National de la Recherche Agronomique (INRA), Centre Auvergne-Rhône-Alpes, site de Theix, Saint-Genès Champanelle, France
- 7 UCIBIO-REQUIMTE, Faculty of Science and Technology, Nova University of Lisbon, Caparica, Portugal
ISSN: 1478-9450
Año de publicación: 2017
Volumen: 14
Número: 10
Páginas: 941-961
Tipo: Artículo
beta Ver similares en nube de resultadosOtras publicaciones en: Expert Review of Proteomics
Resumen
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.