메뉴 건너뛰기




Volumn 58, Issue 3, 2014, Pages 1425-1433

Identification and characterization of a bacitracin resistance network in Enterococcus faecalis

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ALKANAL MONOOXYGENASE (FMN LINKED); AMPICILLIN; BACITRACIN; BETA GALACTOSIDASE; CHLORAMPHENICOL; GALLIDERMIN; LANTIBIOTIC; LINCOMYCIN; MERSACIDIN; NISIN; PENICILLIN G; PROTEOME; TEICOPLANIN; VANCOMYCIN;

EID: 84896892824     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.02111-13     Document Type: Article
Times cited : (48)

References (39)
  • 1
    • 84858398621 scopus 로고    scopus 로고
    • The rise of the Enterococcus: Beyond vancomycin resistance
    • Arias CA, Murray BE. 2012. The rise of the Enterococcus: beyond vancomycin resistance. Nat. Rev. Microbiol. 10:266-278. http://dx.doi.org/10. 1038/nrmicro2761.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 266-278
    • Arias, C.A.1    Murray, B.E.2
  • 2
    • 84879470795 scopus 로고    scopus 로고
    • Undecaprenyl pyrophosphate phosphatase confers low-level resistance to bacitracin in Enterococcus faecalis
    • Shaaly A, Kalamorz F, Gebhard S, Cook GM. 2013. Undecaprenyl pyrophosphate phosphatase confers low-level resistance to bacitracin in Enterococcus faecalis. J. Antimicrob. Chemother. 68:1583-1593. http://dx.doi.org/10.1093/jac/dkt048.
    • (2013) J. Antimicrob. Chemother. , vol.68 , pp. 1583-1593
    • Shaaly, A.1    Kalamorz, F.2    Gebhard, S.3    Cook, G.M.4
  • 3
    • 4644309833 scopus 로고    scopus 로고
    • Acquired bacitracin resistance in Enterococcus faecalis is mediated by an ABC transporter and a novel regulatory protein, BcrR
    • Manson JM, Keis S, Smith JMB, Cook GM. 2004. Acquired bacitracin resistance in Enterococcus faecalis is mediated by an ABC transporter and a novel regulatory protein, BcrR. Antimicrob. Agents Chemother. 48:3743-3748. http://dx.doi.org/10.1128/AAC.48.10.3743-3748.2004.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 3743-3748
    • Manson, J.M.1    Keis, S.2    Smith, J.M.B.3    Cook, G.M.4
  • 4
    • 0032732928 scopus 로고    scopus 로고
    • Defensins and innate host defence of the gastrointestinal tract
    • Bevins CL, Martin-Porter E, Ganz T. 1999. Defensins and innate host defence of the gastrointestinal tract. Gut 45:911-915. http://dx.doi.org/10. 1136/gut.45.6.911.
    • (1999) Gut , vol.45 , pp. 911-915
    • Bevins, C.L.1    Martin-Porter, E.2    Ganz, T.3
  • 5
    • 27244436751 scopus 로고    scopus 로고
    • Food microbiology: Bacteriocins: Developing innate immunity for food
    • DOI 10.1038/nrmicro1273, PII N1273
    • Cotter PD, Hill C, Ross RP. 2005. Bacteriocins: developing innate immunity for food. Nat. Rev. Microbiol. 3:777-788. http://dx.doi.org/10.1038/ nrmicro1273. (Pubitemid 41518738)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.10 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 6
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • DOI 10.1074/jbc.274.13.8405
    • Peschel A, Otto M, Jack RW, Kalbacher H, Jung G, Götz F. 1999. Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J. Biol. Chem. 274:8405-8410. http://dx.doi.org/10.1074/jbc.274.13.8405. (Pubitemid 29164628)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.13 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3    Kalbacher, H.4    Jung, G.5    Gotz, F.6
  • 7
    • 79955769157 scopus 로고    scopus 로고
    • The dlt operon confers resistance to cationic antimicrobial peptides in Clostridium difficile
    • McBride SM, Sonenshein AL. 2011. The dlt operon confers resistance to cationic antimicrobial peptides in Clostridium difficile. Microbiology 157: 1457-1465. http://dx.doi.org/10.1099/mic.0.045997-0.
    • (2011) Microbiology , vol.157 , pp. 1457-1465
    • McBride, S.M.1    Sonenshein, A.L.2
  • 9
    • 0036844128 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis bcrC bacitracin resistance gene by two extracytoplasmic function sigma factors
    • DOI 10.1128/JB.184.22.6123-6129.2002
    • Cao M, Helmann JD. 2002. Regulation of the Bacillus subtilis bcrC bacitracin resistance gene by two extracytoplasmic function sigma factors. J. Bacteriol. 184: 6123-6129. http://dx.doi.org/10.1128/JB.184.22.6123-6129.2002. (Pubitemid 35265892)
    • (2002) Journal of Bacteriology , vol.184 , Issue.22 , pp. 6123-6129
    • Cao, M.1    Helmann, J.D.2
  • 10
    • 0031425436 scopus 로고    scopus 로고
    • Amplification of bacitracin transporter genes in the bacitracin producing Bacillus licheniformis
    • DOI 10.1016/S0378-1097(97)00477-1, PII S0378109797004771
    • Podlesek Z, Herzog B, Comino A. 1997. Amplification of bacitracin transporter genes in the bacitracin producing Bacillus licheniformis. FEMS Microbiol. Lett. 157:201-205. http://dx.doi.org/10.1111/j.1574-6968.1997. tb12774.x. (Pubitemid 28090126)
    • (1997) FEMS Microbiology Letters , vol.157 , Issue.1 , pp. 201-205
    • Podlesek, Z.1    Herzog, B.2    Comino, A.3
  • 11
    • 41749088673 scopus 로고    scopus 로고
    • Bacitracin sensing in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2008.06194.x
    • Rietkötter E, Hoyer D, Mascher T. 2008. Bacitracin sensing in Bacillus subtilis. Mol. Microbiol. 68:768-785. http://dx.doi.org/10.1111/j.1365- 2958.2008.06194.x. (Pubitemid 351490195)
    • (2008) Molecular Microbiology , vol.68 , Issue.3 , pp. 768-785
    • Rietkotter, E.1    Hoyer, D.2    Mascher, T.3
  • 12
    • 78751685410 scopus 로고    scopus 로고
    • Peptide antibiotic sensing and detoxification modules of Bacillus subtili s
    • Staroń A, Finkeisen DE, Mascher T. 2011. Peptide antibiotic sensing and detoxification modules of Bacillus subtili s. Antimicrob. Agents Chemother. 55:515-525. http://dx.doi.org/10.1128/AAC.00352-10.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 515-525
    • Staroń, A.1    Finkeisen, D.E.2    Mascher, T.3
  • 13
    • 84871000484 scopus 로고    scopus 로고
    • ABC transporters of antimicrobial peptides in Firmicutes bacteria - Phylogeny, function and regulation
    • Gebhard S. 2012. ABC transporters of antimicrobial peptides in Firmicutes bacteria - phylogeny, function and regulation. Mol. Microbiol. 86: 1295-1317. http://dx.doi.org/10.1111/mmi.12078.
    • (2012) Mol. Microbiol. , vol.86 , pp. 1295-1317
    • Gebhard, S.1
  • 14
  • 15
    • 0036754861 scopus 로고    scopus 로고
    • Regulatory relationship of two-component and ABC transport systems and clustering of their genes in the Bacillus/Clostridium group, suggest a functional link between them
    • Joseph P, Fichant G, Quentin Y, Denizot F. 2002. Regulatory relationship of two-component and ABC transport systems and clustering of their genes in the Bacillus/Clostridium group, suggest a functional link between them. J. Mol. Microbiol. Biotechnol. 4:503-513. http://www.horizonpress.com/backlist/jmmb/v/ v4/58.pdf. (Pubitemid 35291219)
    • (2002) Journal of Molecular Microbiology and Biotechnology , vol.4 , Issue.5 , pp. 503-513
    • Joseph, P.1    Fichant, G.2    Quentin, Y.3    Denizot, F.4
  • 16
    • 79960409025 scopus 로고    scopus 로고
    • Coevolution of ABC transporters and two-component regulatory systems as resistance modules against antimicrobial peptides in Firmicutes bacteria
    • Dintner S, Staroń A, Berchtold E, Petri T, Mascher T, Gebhard S. 2011. Coevolution of ABC transporters and two-component regulatory systems as resistance modules against antimicrobial peptides in Firmicutes bacteria. J. Bacteriol. 193:3851-3862. http://dx.doi.org/10.1128/JB.05175-11.
    • (2011) J. Bacteriol. , vol.193 , pp. 3851-3862
    • Dintner, S.1    Staroń, A.2    Berchtold, E.3    Petri, T.4    Mascher, T.5    Gebhard, S.6
  • 17
    • 79960702462 scopus 로고    scopus 로고
    • Antimicrobial peptide sensing and detoxification modules: Unravelling the regulatory circuitry of Staphylococcus aureus
    • Gebhard S, Mascher T. 2011. Antimicrobial peptide sensing and detoxification modules: unravelling the regulatory circuitry of Staphylococcus aureus. Mol. Microbiol. 81:581-587. http://dx.doi.org/10.1111/j.1365-2958.2011. 07747.x.
    • (2011) Mol. Microbiol. , vol.81 , pp. 581-587
    • Gebhard, S.1    Mascher, T.2
  • 18
    • 0029189932 scopus 로고
    • Electroporation and efficient transformation of Enterococcus faecalis grown in high concentrations of glycine
    • Shepard BD, Gilmore MS. 1995. Electroporation and efficient transformation of Enterococcus faecalis grown in high concentrations of glycine. Methods Mol. Biol. 47:217-226.
    • (1995) Methods Mol. Biol. , vol.47 , pp. 217-226
    • Shepard, B.D.1    Gilmore, M.S.2
  • 20
    • 0031573015 scopus 로고    scopus 로고
    • A broad-host-range mobilizable shuttle vector for the construction of transcriptional fusions to beta-galactosidase in Gram-positive bacteria
    • DOI 10.1016/S0378-1097(97)00423-0, PII S0378109797004230
    • Poyart C, Trieu-Cuot P. 1997. A broad-host-range mobilizable shuttle vector for the construction of transcriptional fusions to beta-galactosidase in gram-positive bacteria. FEMS Microbiol. Lett. 156:193-198. http://dx.doi.org/10. 1016/S0378-1097(97)00423-0. (Pubitemid 28252818)
    • (1997) FEMS Microbiology Letters , vol.156 , Issue.2 , pp. 193-198
    • Poyart, C.1    Trieu-Cuot, P.2
  • 21
    • 0025334517 scopus 로고
    • A pair of mobilizable shuttle vectors conferring resistance to spectinomycin for molecular cloning in Escherichia coli and in Gram-positive bacteria
    • Trieu-Cuot P, Carlier C, Poyart-Salmeron C, Courvalin P. 1990. A pair of mobilizable shuttle vectors conferring resistance to spectinomycin for molecular cloning in Escherichia coli and in gram-positive bacteria. Nucleic Acids Res. 18:4296. http://dx.doi.org/10.1093/nar/18.14.4296. (Pubitemid 20240267)
    • (1990) Nucleic Acids Research , vol.18 , Issue.14 , pp. 4296
    • Trieu-Cuot, P.1    Carlier, C.2    Poyart-Salmeron, C.3    Courvalin, P.4
  • 23
    • 0033735885 scopus 로고    scopus 로고
    • The CtsR regulator of stress response is active as a dimer and specifically degraded in vivo at 37 degrees C
    • Derré I, Rapoport G, Msadek T. 2000. The CtsR regulator of stress response is active as a dimer and specifically degraded in vivo at 37 degrees C. Mol. Microbiol. 38:335-347. http://dx.doi.org/10.1046/j.1365-2958.2000.02124.x.
    • (2000) Mol. Microbiol. , vol.38 , pp. 335-347
    • Derré, I.1    Rapoport, G.2    Msadek, T.3
  • 24
    • 34548857194 scopus 로고    scopus 로고
    • MIT Artificial Intelligence Laboratory, MIT Synthetic Biology Working Group, Massachusetts Institute of Technology, Cambridge, MA
    • Knight T. Idempotent vector design for standard assembly of BioBricks. MIT Artificial Intelligence Laboratory, MIT Synthetic Biology Working Group, Massachusetts Institute of Technology, Cambridge, MA.
    • Idempotent Vector Design for Standard Assembly of BioBricks
    • Knight, T.1
  • 26
    • 70350434311 scopus 로고    scopus 로고
    • Capsular polysaccharide production in Enterococcus faecalis and contribution of CpsF to capsule serospecificity
    • Thurlow LR, Thomas VC, Hancock LE. 2009. Capsular polysaccharide production in Enterococcus faecalis and contribution of CpsF to capsule serospecificity. J. Bacteriol. 191:6203-6210. http://dx.doi.org/10.1128/JB. 00592-09.
    • (2009) J. Bacteriol. , vol.191 , pp. 6203-6210
    • Thurlow, L.R.1    Thomas, V.C.2    Hancock, L.E.3
  • 27
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • DOI 10.1016/0378-1119(89)90358-2
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59. http://dx.doi.org/10.1016/0378-1119(89)90358-2. (Pubitemid 19125653)
    • (1989) Gene , vol.77 , Issue.1 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 28
    • 43749121632 scopus 로고    scopus 로고
    • Molecular analysis of BcrR, a membrane-bound bacitracin sensor and DNA-binding protein from Enterococcus faecalis
    • Gauntlett JC, Gebhard S, Keis S, Manson JM, Pos KM, Cook GM. 2008. Molecular analysis of BcrR, a membrane-bound bacitracin sensor and DNA-binding protein from Enterococcus faecalis. J. Biol. Chem. 283:8591-8600. http://dx.doi.org/10.1074/jbc.M709503200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8591-8600
    • Gauntlett, J.C.1    Gebhard, S.2    Keis, S.3    Manson, J.M.4    Pos, K.M.5    Cook, G.M.6
  • 30
    • 33750953585 scopus 로고    scopus 로고
    • The Phn system of Mycobacterium smegmatis: A second high-affinity ABC-transporter for phosphate
    • DOI 10.1099/mic.0.29201-0
    • Gebhard S, Tran SL, Cook GM. 2006. The Phn system of Mycobacterium smegmatis: a second high-affinity ABC-transporter for phosphate. Microbiology 152:3453-3465. http://dx.doi.org/10.1099/mic.0.29201-0. (Pubitemid 44734346)
    • (2006) Microbiology , vol.152 , Issue.11 , pp. 3453-3465
    • Gebhard, S.1    Tran, S.L.2    Cook, G.M.3
  • 31
    • 84877127954 scopus 로고    scopus 로고
    • Characterization of a regulatory network of peptide antibiotic detoxification modules in Lactobacillus casei BL23
    • Revilla-Guarinos A, Gebhard S, Alcántara C, Staroń A, Mascher T, Zúñiga M. 2013. Characterization of a regulatory network of peptide antibiotic detoxification modules in Lactobacillus casei BL23. Appl. Environ. Microbiol. 79:3160-3170. http://dx.doi.org/10.1128/AEM.00178-13.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 3160-3170
    • Revilla-Guarinos, A.1    Gebhard, S.2    Alcántara, C.3    Staroń, A.4    Mascher, T.5    Zúñiga, M.6
  • 32
    • 79960701758 scopus 로고    scopus 로고
    • Bacitracin and nisin resistance in Staphylococcus aureus: A novel pathway involving the BraS/BraR two-component system (SA2417/SA2418) and both the BraD/BraE and VraD/VraE ABC transporters
    • Hiron A, Falord M, Valle J, Débarbouillé M, Msadek T. 2011. Bacitracin and nisin resistance in Staphylococcus aureus: a novel pathway involving the BraS/BraR two-component system (SA2417/SA2418) and both the BraD/BraE and VraD/VraE ABC transporters. Mol. Microbiol. 81:602-622. http://dx.doi.org/10.1111/j.1365-2958.2011.07735.x.
    • (2011) Mol. Microbiol. , vol.81 , pp. 602-622
    • Hiron, A.1    Falord, M.2    Valle, J.3    Débarbouillé, M.4    Msadek, T.5
  • 33
    • 0041528524 scopus 로고    scopus 로고
    • The BceRS two-component regulatory system induces expression of the bacitracin transporter, BceAB, in Bacillus subtilis
    • Ohki R, Giyanto, Tateno K, Masuyama W, Moriya S, Kobayashi K, Ogasawara N. 2003. The BceRS two-component regulatory system induces expression of the bacitracin transporter, BceAB, in Bacillus subtilis. Mol. Microbiol. 49:1135-1144. http://dx.doi.org/10.1046/j.1365-2958.2003.03653.x.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1135-1144
    • Ohki, R.1    Giyanto2    Tateno, K.3    Masuyama, W.4    Moriya, S.5    Kobayashi, K.6    Ogasawara, N.7
  • 35
    • 0034616961 scopus 로고    scopus 로고
    • Acetyl phosphate-dependent activation of a mutant PhoP response regulator that functions independently of its cognate sensor kinase
    • Chamnongpol S, Groisman EA. 2000. Acetyl phosphate-dependent activation of a mutant PhoP response regulator that functions independently of its cognate sensor kinase. J. Mol. Biol. 300:291-305. http://dx.doi.org/10.1006/jmbi.2000. 3848.
    • (2000) J. Mol. Biol. , vol.300 , pp. 291-305
    • Chamnongpol, S.1    Groisman, E.A.2
  • 36
    • 84873433178 scopus 로고    scopus 로고
    • Stoichiometry and perturbation studies of the LiaFSR system of Bacillus subtilis
    • Schrecke K, Jordan S, Mascher T. 2013. Stoichiometry and perturbation studies of the LiaFSR system of Bacillus subtilis. Mol. Microbiol. 87:769-788. http://dx.doi.org/10.1111/mmi.12130.
    • (2013) Mol. Microbiol. , vol.87 , pp. 769-788
    • Schrecke, K.1    Jordan, S.2    Mascher, T.3
  • 37
    • 37349034233 scopus 로고    scopus 로고
    • Cell envelope stress response in Gram-positive bacteria
    • DOI 10.1111/j.1574-6976.2007.00091.x
    • Jordan S, Hutchings MI, Mascher T. 2008. Cell envelope stress response in Gram-positive bacteria. FEMS Microbiol. Rev. 32:107-146. http://dx.doi.org/10. 1111/j.1574-6976.2007.00091.x. (Pubitemid 350293914)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.1 , pp. 107-146
    • Jordan, S.1    Hutchings, M.I.2    Mascher, T.3
  • 38
    • 84856069886 scopus 로고    scopus 로고
    • GraXSR proteins interact with the VraFG ABC transporter to form a five-component system required for cationic antimicrobial peptide sensing and resistance in Staphylococcus aureus
    • Falord M, Karimova G, Hiron A, Msadek T. 2012. GraXSR proteins interact with the VraFG ABC transporter to form a five-component system required for cationic antimicrobial peptide sensing and resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 56:1047-1058. http://dx.doi.org/10.1128/AAC.05054- 11.
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 1047-1058
    • Falord, M.1    Karimova, G.2    Hiron, A.3    Msadek, T.4
  • 39
    • 36148999436 scopus 로고    scopus 로고
    • The antimicrobial peptide-sensing system aps of Staphylococcus aureus
    • DOI 10.1111/j.1365-2958.2007.05986.x
    • Li M, Cha DJ, Lai Y, Villaruz AE, Sturdevant DE, Otto M. 2007. The antimicrobial peptide-sensing system aps of Staphylococcus aureus. Mol. Microbiol. 66:1136-1147. http://dx.doi.org/10.1111/j.1365-2958.2007.05986.x. (Pubitemid 350115022)
    • (2007) Molecular Microbiology , vol.66 , Issue.5 , pp. 1136-1147
    • Li, M.1    Cha, D.J.2    Lai, Y.3    Villaruz, A.E.4    Sturdevant, D.E.5    Otto, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.