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Subproteomic signature comparison of in vitro selected fluoroquinolone resistance and ciprofloxacin stress in Salmonella Typhimurium DT104B.

Subproteomic signature comparison of in vitro selected fluoroquinolone resistance and ciprofloxacin stress in Salmonella Typhimurium DT104B.
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Correia S, Hébraud M, Chafsey I, Chambon C, Viala D, Torres C, Caniça M, Capelo JL, Poeta P, Igrejas G,


Correia S, Hébraud M, Chafsey I, Chambon C, Viala D, Torres C, Caniça M, Capelo JL, Poeta P, Igrejas G, (click to view)

Correia S, Hébraud M, Chafsey I, Chambon C, Viala D, Torres C, Caniça M, Capelo JL, Poeta P, Igrejas G,

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Expert review of proteomics 2017 09 05() doi 10.1080/14789450.2017.1375856

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.

AIM AND METHODS
To evaluate 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, 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.

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