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. 2018 Aug 27;62(9):e00906-18.
doi: 10.1128/AAC.00906-18. Print 2018 Sep.

Functional Characterization of AbaQ, a Novel Efflux Pump Mediating Quinolone Resistance in Acinetobacter baumannii

María Pérez-Varela  1 , Jordi Corral  1 , Jesús Aranda  2 , Jordi Barbé  1
Affiliations

Functional Characterization of AbaQ, a Novel Efflux Pump Mediating Quinolone Resistance in Acinetobacter baumannii

María Pérez-Varela et al. Antimicrob Agents Chemother. .

Abstract

Acinetobacter baumannii has emerged as an important multidrug-resistant nosocomial pathogen. In previous work, we identified a putative MFS transporter, AU097_RS17040, involved in the pathogenicity of A. baumannii (M. Pérez-Varela, J. Corral, J. A. Vallejo, S. Rumbo-Feal, G. Bou, J. Aranda, and J. Barbé, Infect Immun 85:e00327-17, 2017, https://doi.org/10.1128/IAI.00327-17). In this study, we analyzed the susceptibility to diverse antimicrobial agents of A. baumannii cells defective in this transporter, referred to as AbaQ. Our results showed that AbaQ is mainly involved in the extrusion of quinolone-type drugs in A. baumannii.

Keywords: Acinetobacter; efflux pumps; quinolones.

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Figures

FIG 1
FIG 1
(A) Prediction of the structure of AbaQ using Protter (10). The putative protein is shown parallel to the cytoplasmic membrane. (B) 3D representation of AbaQ viewed along the plane of the membrane from the periplasmic side using RaptorX Structure Prediction (26) and visualized using PyMOL software (27). The 12 transmembrane α-helices are numbered (1 to 12); both the N and C termini are located in the cytoplasm.
See this image and copyright information in PMC

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