Correia, SusanaHébraud, MichelChafsey, IngridChambon, ChristopheViala, DidierTorres, CarmenCaniça, ManuelaCapelo, José LuisPoeta, PatríciaIgrejas, Gilberto2018-03-072018-03-072017-10Expert Rev Proteomics. 2017 Oct;14(10):941-961. doi: 10.1080/14789450.2017.1375856. Epub 2017 Sep 18.1478-9450http://hdl.handle.net/10400.18/5355Background: 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.engAntimicrobial ResistanceComparative SubproteomicsLC-MS/MSSalmonella Typhimurium DT104BShotgun Proteomics2-DEResistência aos Antimicrobianosjournal article10.1080/14789450.2017.1375856