메뉴 건너뛰기




Volumn 75, Issue 9, 2012, Pages 2638-2648

Downregulation of Na(+)-NQR complex is essential for Vibrio alginolyticus in resistance to balofloxacin

Author keywords

Antibiotic resistance; Balofloxacin; Metabolic regulation; Na(+) NQR; Proteomics; Vibro alginolyticus

Indexed keywords

BALOFLOXACIN; TOLC PROTEIN;

EID: 84860438183     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.03.006     Document Type: Article
Times cited : (24)

References (41)
  • 2
    • 55449137075 scopus 로고    scopus 로고
    • Role of RpoS in stress survival, synthesis of extracellular autoinducer 2, and virulence in Vibrio alginolyticus
    • Tian Y., Wang Q.Y., Liu Q., Ma Y., Cao X.D., Zhang Y.X. Role of RpoS in stress survival, synthesis of extracellular autoinducer 2, and virulence in Vibrio alginolyticus. Arch Microbiol 2008, 190:585-594.
    • (2008) Arch Microbiol , vol.190 , pp. 585-594
    • Tian, Y.1    Wang, Q.Y.2    Liu, Q.3    Ma, Y.4    Cao, X.D.5    Zhang, Y.X.6
  • 3
    • 40849085083 scopus 로고    scopus 로고
    • Vibrios in association with sedimentary crustaceans in three beaches of the northern Adriatic Sea (Italy)
    • Harriague A.C., Di Brino M., Zampini M., Albertelli G., Pruzzo C., Misic C. Vibrios in association with sedimentary crustaceans in three beaches of the northern Adriatic Sea (Italy). Mar Pollut Bull 2008, 56:574-579.
    • (2008) Mar Pollut Bull , vol.56 , pp. 574-579
    • Harriague, A.C.1    Di Brino, M.2    Zampini, M.3    Albertelli, G.4    Pruzzo, C.5    Misic, C.6
  • 4
    • 13544253591 scopus 로고    scopus 로고
    • Antibiotic resistance in Aeromonas hydrophila and Vibrio alginolyticus isolated from a wound infection: a case report
    • Horii T., Morita M., Muramatsu H., Monji A., Miyagishima D., Kanno T., et al. Antibiotic resistance in Aeromonas hydrophila and Vibrio alginolyticus isolated from a wound infection: a case report. J Trauma 2005, 58:196-200.
    • (2005) J Trauma , vol.58 , pp. 196-200
    • Horii, T.1    Morita, M.2    Muramatsu, H.3    Monji, A.4    Miyagishima, D.5    Kanno, T.6
  • 5
    • 79951979473 scopus 로고    scopus 로고
    • Antimicrobial resistance of Vibrio parahaemolyticus and Vibrio alginolyticus strains isolated from farmed fish in Korea from 2005 through 2007
    • Oh E.G., Son K.T., Yu H., Lee T.S., Lee H.J., Shin S., et al. Antimicrobial resistance of Vibrio parahaemolyticus and Vibrio alginolyticus strains isolated from farmed fish in Korea from 2005 through 2007. J Food Prot 2011, 74:380-386.
    • (2011) J Food Prot , vol.74 , pp. 380-386
    • Oh, E.G.1    Son, K.T.2    Yu, H.3    Lee, T.S.4    Lee, H.J.5    Shin, S.6
  • 6
    • 50249152982 scopus 로고    scopus 로고
    • Distribution of some virulence related-properties of Vibrio alginolyticus strains isolated from Mediterranean seawater (Bay of Khenis, Tunisia): investigation of eight Vibrio cholerae virulence genes
    • Snoussi M., Noumi E., Usai D., Sechi L.A., Zanetti S., Bakhrouf A. Distribution of some virulence related-properties of Vibrio alginolyticus strains isolated from Mediterranean seawater (Bay of Khenis, Tunisia): investigation of eight Vibrio cholerae virulence genes. World J Microbiol Biotechnol 2008, 24:2133-2141.
    • (2008) World J Microbiol Biotechnol , vol.24 , pp. 2133-2141
    • Snoussi, M.1    Noumi, E.2    Usai, D.3    Sechi, L.A.4    Zanetti, S.5    Bakhrouf, A.6
  • 7
    • 78649652049 scopus 로고    scopus 로고
    • Differentially expressed outer membrane proteins of Vibrio alginolyticus in response to six types of antibiotics
    • Xiong P., Wang C., Ye M.Z., Yang T.C., Peng X.X., Li H. Differentially expressed outer membrane proteins of Vibrio alginolyticus in response to six types of antibiotics. Mar Biotechnol 2010, 12:686-695.
    • (2010) Mar Biotechnol , vol.12 , pp. 686-695
    • Xiong, P.1    Wang, C.2    Ye, M.Z.3    Yang, T.C.4    Peng, X.X.5    Li, H.6
  • 8
    • 81055156017 scopus 로고    scopus 로고
    • Proteomics and biomarkers in clinical trials for drug development
    • Lee J.M., Han J.J., Altwerger G., Kohn E.C. Proteomics and biomarkers in clinical trials for drug development. J Proteomics 2011, 74:2632-2641.
    • (2011) J Proteomics , vol.74 , pp. 2632-2641
    • Lee, J.M.1    Han, J.J.2    Altwerger, G.3    Kohn, E.C.4
  • 9
    • 79959543603 scopus 로고    scopus 로고
    • Non-adaptive origins of interactome complexity
    • Fernandez A., Lynch M. Non-adaptive origins of interactome complexity. Nature 2011, 474:502-U130.
    • (2011) Nature , vol.474
    • Fernandez, A.1    Lynch, M.2
  • 11
    • 79961000138 scopus 로고    scopus 로고
    • Proteomic comparison of etioplast and chloroplast protein complexes
    • Plöscher M., Reisinger V., Eichacker L.A. Proteomic comparison of etioplast and chloroplast protein complexes. J Proteomics 2011, 74:1256-1265.
    • (2011) J Proteomics , vol.74 , pp. 1256-1265
    • Plöscher, M.1    Reisinger, V.2    Eichacker, L.A.3
  • 13
    • 33745160404 scopus 로고    scopus 로고
    • Large-scale identification of protein-protein interaction of Escherichia coli K-12
    • Arifuzzaman M., Maeda M., Itoh A., Nishikata K., Takita C., Saito R., et al. Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 2006, 16:686-691.
    • (2006) Genome Res , vol.16 , pp. 686-691
    • Arifuzzaman, M.1    Maeda, M.2    Itoh, A.3    Nishikata, K.4    Takita, C.5    Saito, R.6
  • 14
    • 13444283630 scopus 로고    scopus 로고
    • Interaction network containing conserved and essential protein complexes in Escherichia coli
    • Butland G., Peregrin-Alvarez J.M., Li J., Yang W., Yang X., Canadien V., et al. Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 2005, 433:531-538.
    • (2005) Nature , vol.433 , pp. 531-538
    • Butland, G.1    Peregrin-Alvarez, J.M.2    Li, J.3    Yang, W.4    Yang, X.5    Canadien, V.6
  • 15
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger H., von Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem 1991, 199:223-231.
    • (1991) Anal Biochem , vol.199 , pp. 223-231
    • Schägger, H.1    von Jagow, G.2
  • 16
    • 28444497467 scopus 로고    scopus 로고
    • Advantages and limitations of clear-native PAGE
    • Wittig L., Schagger H. Advantages and limitations of clear-native PAGE. Proteomics 2005, 5:4338-4346.
    • (2005) Proteomics , vol.5 , pp. 4338-4346
    • Wittig, L.1    Schagger, H.2
  • 17
    • 80051754003 scopus 로고    scopus 로고
    • Complexome of Escherichia coli cytosolic proteins under normal natural conditions
    • Pan J.Y., Wu H.K., Liu X., Li P.P., Li H., Wang S.Y., et al. Complexome of Escherichia coli cytosolic proteins under normal natural conditions. Mol Biosyst 2011, 7:2651-2663.
    • (2011) Mol Biosyst , vol.7 , pp. 2651-2663
    • Pan, J.Y.1    Wu, H.K.2    Liu, X.3    Li, P.P.4    Li, H.5    Wang, S.Y.6
  • 18
    • 77954381798 scopus 로고    scopus 로고
    • Complexome of Escherichia coli envelope proteins under normal physiological conditions
    • Pan J.Y., Li H., Ma Y., Chen P., Zhao P., Wang S.Y., et al. Complexome of Escherichia coli envelope proteins under normal physiological conditions. J Proteome Res 2010, 9:3730-3740.
    • (2010) J Proteome Res , vol.9 , pp. 3730-3740
    • Pan, J.Y.1    Li, H.2    Ma, Y.3    Chen, P.4    Zhao, P.5    Wang, S.Y.6
  • 19
    • 33845382343 scopus 로고    scopus 로고
    • Systematic identification of the subproteome of Escherichia coli cell envelope reveals the interaction network of membrane proteins and membrane-associated peripheral proteins
    • Huang C.Z., Lin X.M., Wu L.N., Zhang D.F., Liu D., Wang S.Y., et al. Systematic identification of the subproteome of Escherichia coli cell envelope reveals the interaction network of membrane proteins and membrane-associated peripheral proteins. J Proteome Res 2006, 5:3268-3276.
    • (2006) J Proteome Res , vol.5 , pp. 3268-3276
    • Huang, C.Z.1    Lin, X.M.2    Wu, L.N.3    Zhang, D.F.4    Liu, D.5    Wang, S.Y.6
  • 20
    • 79960939536 scopus 로고    scopus 로고
    • Metabolic regulation of antibiotic resistance
    • Martínez J.L., Rojo F. Metabolic regulation of antibiotic resistance. FEMS Microbiol Rev 2011, 35(5):768-789.
    • (2011) FEMS Microbiol Rev , vol.35 , Issue.5 , pp. 768-789
    • Martínez, J.L.1    Rojo, F.2
  • 21
    • 66149119794 scopus 로고    scopus 로고
    • Gatifloxacin, moxifloxacin, and balofloxacin resistance due to mutations in the gyrA and parC genes of Staphylococcus epidermidis strains Isolated from patients with endophthalmitis, corneal ulcers and conjunctivitis
    • Betanzos-Cabrera G., Juarez-Verdayes M.A., Gonzalez-Gonzalez G., Cancino-Diaz M.E., Cancino-Diaz J.C. Gatifloxacin, moxifloxacin, and balofloxacin resistance due to mutations in the gyrA and parC genes of Staphylococcus epidermidis strains Isolated from patients with endophthalmitis, corneal ulcers and conjunctivitis. Ophthalmic Res 2009, 42:43-48.
    • (2009) Ophthalmic Res , vol.42 , pp. 43-48
    • Betanzos-Cabrera, G.1    Juarez-Verdayes, M.A.2    Gonzalez-Gonzalez, G.3    Cancino-Diaz, M.E.4    Cancino-Diaz, J.C.5
  • 22
    • 82955206474 scopus 로고    scopus 로고
    • Mechanisms of fluoroquinolone resistance in Escherichia coli isolates from food-producing animals
    • Karczmarczyk M., Martins M., Quinn T., Leonard N., Fanning S. Mechanisms of fluoroquinolone resistance in Escherichia coli isolates from food-producing animals. Appl Environ Microbiol 2011, 77:7113-7120.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 7113-7120
    • Karczmarczyk, M.1    Martins, M.2    Quinn, T.3    Leonard, N.4    Fanning, S.5
  • 23
    • 70349898789 scopus 로고    scopus 로고
    • Identification of broad cross-protective immunogens using heterogeneous antiserum-based immunoproteomic approach
    • Li H., Xiong X.P., Peng B., Xu C.X., Ye M.Z., Yang T.C., et al. Identification of broad cross-protective immunogens using heterogeneous antiserum-based immunoproteomic approach. J Proteome Res 2009, 8:4342-4349.
    • (2009) J Proteome Res , vol.8 , pp. 4342-4349
    • Li, H.1    Xiong, X.P.2    Peng, B.3    Xu, C.X.4    Ye, M.Z.5    Yang, T.C.6
  • 24
    • 85184287028 scopus 로고    scopus 로고
    • Determination of the heterogeneous interactome between Edwardsiella tarda and fish gills
    • Liu Y, Zhang HL, Liu YJ, Li H, Peng XX. Determination of the heterogeneous interactome between Edwardsiella tarda and fish gills. J Proteomics.
    • J Proteomics.
    • Liu, Y.1    Zhang, H.L.2    Liu, Y.J.3    Li, H.4    Peng, X.X.5
  • 25
    • 84855873103 scopus 로고    scopus 로고
    • Identification of plasma-responsive outer membrane proteins and their vaccine potential in Edwardsiella tarda using proteomic approach
    • Wang C, Liu YJ, Li H, Xu WJ, Zhang HL, Peng XX. Identification of plasma-responsive outer membrane proteins and their vaccine potential in Edwardsiella tarda using proteomic approach. J Proteomics.
    • J Proteomics.
    • Wang, C.1    Liu, Y.J.2    Li, H.3    Xu, W.J.4    Zhang, H.L.5    Peng, X.X.6
  • 26
    • 55249089247 scopus 로고    scopus 로고
    • Identification and network of outer membrane proteins regulating streptomycin-resistance in Escherichia coli
    • Li H., Wang B.C., Xu W.J., Lin X.M., Peng X.X. Identification and network of outer membrane proteins regulating streptomycin-resistance in Escherichia coli. J Proteome Res 2008, 7:4040-4049.
    • (2008) J Proteome Res , vol.7 , pp. 4040-4049
    • Li, H.1    Wang, B.C.2    Xu, W.J.3    Lin, X.M.4    Peng, X.X.5
  • 29
    • 0032946957 scopus 로고    scopus 로고
    • Using native gel in two-dimensional PAGE for the detection of protein interactions in protein extract
    • Sun H., Pan Y.C. Using native gel in two-dimensional PAGE for the detection of protein interactions in protein extract. J Biochem Biophys Methods 1999, 39:143-151.
    • (1999) J Biochem Biophys Methods , vol.39 , pp. 143-151
    • Sun, H.1    Pan, Y.C.2
  • 30
    • 77955445442 scopus 로고    scopus 로고
    • Energy transducing redox steps of the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae
    • Juárez O., Morgan J.E., Nilges M.J., Barquera B. Energy transducing redox steps of the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae. Proc Natl Acad Sci U S A 2010, 107:12505-12510.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 12505-12510
    • Juárez, O.1    Morgan, J.E.2    Nilges, M.J.3    Barquera, B.4
  • 31
    • 49849089764 scopus 로고    scopus 로고
    • Proteomic analysis of nalidixic acid resistance in Escherichia coli: identification and functional characterization of OM proteins
    • Lin X.M., Li H., Wang C., Peng X.X. Proteomic analysis of nalidixic acid resistance in Escherichia coli: identification and functional characterization of OM proteins. J Proteome Res 2008, 7:2399-2405.
    • (2008) J Proteome Res , vol.7 , pp. 2399-2405
    • Lin, X.M.1    Li, H.2    Wang, C.3    Peng, X.X.4
  • 32
    • 79952802131 scopus 로고    scopus 로고
    • The third-generation P-glycoprotein inhibitor tariquidar may overcome bacterial multidrug resistance by increasing intracellular drug concentration
    • Leitner I., Nemeth J., Feurstein T., Abrahim A., Matzneller P. The third-generation P-glycoprotein inhibitor tariquidar may overcome bacterial multidrug resistance by increasing intracellular drug concentration. J Antimicrob Chemother 2011, 66:834-839.
    • (2011) J Antimicrob Chemother , vol.66 , pp. 834-839
    • Leitner, I.1    Nemeth, J.2    Feurstein, T.3    Abrahim, A.4    Matzneller, P.5
  • 33
    • 79955628177 scopus 로고    scopus 로고
    • Characterization of the E506Q and H537A dysfunctional mutants in the E. coli ABC transporter MsbA
    • Schultz K.M., Merten J.A., Klug C.S. Characterization of the E506Q and H537A dysfunctional mutants in the E. coli ABC transporter MsbA. Biochemistry 2011, 50:3599-3608.
    • (2011) Biochemistry , vol.50 , pp. 3599-3608
    • Schultz, K.M.1    Merten, J.A.2    Klug, C.S.3
  • 34
    • 79953649285 scopus 로고    scopus 로고
    • Multidrug resistance ABC transporter structure predictions by homology modeling approaches
    • Honorat M., Falson P., Terreux R., Di Pietro A., Dumontet C., Payen L. Multidrug resistance ABC transporter structure predictions by homology modeling approaches. Curr Drug Metab 2011, 12:268-277.
    • (2011) Curr Drug Metab , vol.12 , pp. 268-277
    • Honorat, M.1    Falson, P.2    Terreux, R.3    Di Pietro, A.4    Dumontet, C.5    Payen, L.6
  • 35
    • 33646258235 scopus 로고    scopus 로고
    • An important role of a "probable ATP-binding component of ABC transporter" during the process of Pseudomonas aeruginosa resistance to fluoroquinolone
    • Zhou J., Hao D., Wang X., Liu T., He C., Xie F., et al. An important role of a "probable ATP-binding component of ABC transporter" during the process of Pseudomonas aeruginosa resistance to fluoroquinolone. Proteomics 2006, 6:2495-2503.
    • (2006) Proteomics , vol.6 , pp. 2495-2503
    • Zhou, J.1    Hao, D.2    Wang, X.3    Liu, T.4    He, C.5    Xie, F.6
  • 37
    • 79551494258 scopus 로고    scopus 로고
    • The sensor kinase CbrA is a global regulator that modulates metabolism, virulence, and antibiotic resistance in Pseudomonas aeruginosa
    • Yeung A.T., Bains M., Hancock R.E. The sensor kinase CbrA is a global regulator that modulates metabolism, virulence, and antibiotic resistance in Pseudomonas aeruginosa. J Bacteriol 2011, 193:918-931.
    • (2011) J Bacteriol , vol.193 , pp. 918-931
    • Yeung, A.T.1    Bains, M.2    Hancock, R.E.3
  • 38
    • 79955886933 scopus 로고    scopus 로고
    • Metabolite-enabled eradication of bacterial persisters by aminoglycosides
    • Allison K.R., Brynildsen M.P., Collins J.J. Metabolite-enabled eradication of bacterial persisters by aminoglycosides. Nature 2011, 473:216-220.
    • (2011) Nature , vol.473 , pp. 216-220
    • Allison, K.R.1    Brynildsen, M.P.2    Collins, J.J.3
  • 39
    • 81155126113 scopus 로고    scopus 로고
    • Localization of ubiquinone-8 in the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae
    • Casutt M.S., Nedielkov R., Wendelspiess S., Vossler S., Gerken U., Murai M., et al. Localization of ubiquinone-8 in the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae. J Biol Chem 2011, 18:40075-40082.
    • (2011) J Biol Chem , vol.18 , pp. 40075-40082
    • Casutt, M.S.1    Nedielkov, R.2    Wendelspiess, S.3    Vossler, S.4    Gerken, U.5    Murai, M.6
  • 40
    • 34548667971 scopus 로고    scopus 로고
    • Regulation of expression of Na+-translocating NADH:quinone oxidoreductase genes in Vibrio harveyi and Klebsiella pneumoniae
    • Fadeeva M.S., Yakovtseva E.A., Belevich G.A., Bertsova Y.V., Bogachev A. Regulation of expression of Na+-translocating NADH:quinone oxidoreductase genes in Vibrio harveyi and Klebsiella pneumoniae. Arch Microbiol 2007, 188:341-348.
    • (2007) Arch Microbiol , vol.188 , pp. 341-348
    • Fadeeva, M.S.1    Yakovtseva, E.A.2    Belevich, G.A.3    Bertsova, Y.V.4    Bogachev, A.5
  • 41
    • 80053901787 scopus 로고    scopus 로고
    • Combination therapies for combating antimicrobial resistance
    • Fischbach M.A. Combination therapies for combating antimicrobial resistance. Curr Opin Microbiol 2011, 14:519-523.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 519-523
    • Fischbach, M.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.