Role of H- and D- MATE-Type Transporters from Multidrug Resistant Clinical Isolates of Vibrio fluvialis in Conferring Fluoroquinolone Resistance

Mohanty, Priyabrata; Patel, Arati; Bhardwaj, Ashima Kushwaha

doi:10.1371/journal.pone.0035752

Cited by 21 publications

(27 citation statements)

References 22 publications

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“…It was reported that the thiolate forms at the nucleophilic cysteine residues (Cys30 in the Ec DsbA numbering) are stabilized in reduced forms of Ec DsbA and Vibrio cholera DsbA ( Guddat et al, 1998 ; Mohanty et al, 2012 ). The stabilization of the thiolate forms were suggested to result from the interactions within the C XX C moitf ( Guddat et al, 1998 ).…”

Section: Resultsmentioning

confidence: 99%

Crystal Structure of DsbA from Corynebacterium diphtheriae and Its Functional Implications for CueP in Gram-Positive Bacteria

Sh¹,

Kim²,

Song³

et al. 2015

Molecules and Cells

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In Gram-negative bacteria in the periplasmic space, the dimeric thioredoxin-fold protein DsbC isomerizes and reduces incorrect disulfide bonds of unfolded proteins, while the monomeric thioredoxin-fold protein DsbA introduces disulfide bonds in folding proteins. In the Gram-negative bacteria Salmonella enterica serovar Typhimurium, the reduced form of CueP scavenges the production of hydroxyl radicals in the copper-mediated Fenton reaction, and DsbC is responsible for keeping CueP in the reduced, active form. Some DsbA proteins fulfill the functions of DsbCs, which are not present in Gram-positive bacteria. In this study, we identified a DsbA homologous protein (CdDsbA) in the Corynebacterium diphtheriae genome and determined its crystal structure in the reduced condition at 1.5 Å resolution. CdDsbA consists of a monomeric thioredoxin-like fold with an inserted helical domain and unique N-terminal extended region. We confirmed that CdDsbA has disulfide bond isomerase/reductase activity, and we present evidence that the N-terminal extended region is not required for this activity and folding of the core DsbA-like domain. Furthermore, we found that CdDsbA could reduce CueP from C. diphtheriae.

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Section: Resultsmentioning

confidence: 99%

Crystal Structure of DsbA from Corynebacterium diphtheriae and Its Functional Implications for CueP in Gram-Positive Bacteria

Sh¹,

Kim²,

Song³

et al. 2015

Molecules and Cells

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“…V. parahaemolyticus was the organism in which the first MATE family transporter, NorM, was discovered by cloning in E. coli (353), and in V. cholerae, 5 members of this family were described (16), including the NorM homolog VcmA (15), which increases MICs of fluoroquinolones, ethidium bromide, acriflavine, and doxorubicin when overproduced in E. coli. Two MATE transporters from a multidrug-resistant V. fluvialis isolate provided 2-fold increases in MIC values of ciprofloxacin and norfloxacin when expressed in E. coli (354).…”

Section: Vibrio Sppmentioning

confidence: 99%

The Challenge of Efflux-Mediated Antibiotic Resistance in Gram-Negative Bacteria

2015

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SUMMARY The global emergence of multidrug-resistant Gram-negative bacteria is a growing threat to antibiotic therapy. The chromosomally encoded drug efflux mechanisms that are ubiquitous in these bacteria greatly contribute to antibiotic resistance and present a major challenge for antibiotic development. Multidrug pumps, particularly those represented by the clinically relevant AcrAB-TolC and Mex pumps of the resistance-nodulation-division (RND) superfamily, not only mediate intrinsic and acquired multidrug resistance (MDR) but also are involved in other functions, including the bacterial stress response and pathogenicity. Additionally, efflux pumps interact synergistically with other resistance mechanisms (e.g., with the outer membrane permeability barrier) to increase resistance levels. Since the discovery of RND pumps in the early 1990s, remarkable scientific and technological advances have allowed for an in-depth understanding of the structural and biochemical basis, substrate profiles, molecular regulation, and inhibition of MDR pumps. However, the development of clinically useful efflux pump inhibitors and/or new antibiotics that can bypass pump effects continues to be a challenge. Plasmid-borne efflux pump genes (including those for RND pumps) have increasingly been identified. This article highlights the recent progress obtained for organisms of clinical significance, together with methodological considerations for the characterization of MDR pumps.

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“…As reported, MATE family efflux pumps depend upon Na+/H+ gradient for transport and have three major branches: the NorM branch, a branch containing several eukaryotic proteins and a branch containing E. coli DinF (Mohanty et al, 2012). MATE protein length varies from 400 to 700 residues comprising of 12 transmembrane helices.…”

Section: Introductionmentioning

confidence: 98%

“…MATE transporters confer resistance to bacterial pathogens and cancer cells, thus causing critical reductions in the curative efficacies of antibiotics and anti-cancer drugs, respectively (Tanaka et al, 2013). An example of one such protein is NorM, of Vibrio parahaemolyticus which is a multidrug Na +-antiporter, and was found to confer resistance to dyes, fluoroquinolones and aminoglycosides (Mohanty et al, 2012;Li and Nikaido, 2004).…”

Section: Introductionmentioning

confidence: 99%

MATEPRED-A-SVM-Based Prediction Method for Multidrug And Toxin Extrusion (MATE) Proteins

Tamanna

Ramana

2015

Computational Biology and Chemistry

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Role of H- and D- MATE-Type Transporters from Multidrug Resistant Clinical Isolates of Vibrio fluvialis in Conferring Fluoroquinolone Resistance

Cited by 21 publications

References 22 publications

Crystal Structure of DsbA from Corynebacterium diphtheriae and Its Functional Implications for CueP in Gram-Positive Bacteria

Crystal Structure of DsbA from Corynebacterium diphtheriae and Its Functional Implications for CueP in Gram-Positive Bacteria

The Challenge of Efflux-Mediated Antibiotic Resistance in Gram-Negative Bacteria

MATEPRED-A-SVM-Based Prediction Method for Multidrug And Toxin Extrusion (MATE) Proteins

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