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Volumn 181, Issue 12, 1999, Pages 3644-3648

Characterization of the vanD glycopeptide resistance gene cluster from Enterococcus faecium BM4339

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMPICILLIN; CARBOXYPEPTIDASE; DIPEPTIDASE; GLYCOPEPTIDE; KANAMYCIN; LIGASE; OXIDOREDUCTASE; PENICILLIN BINDING PROTEIN; PEPTIDOGLYCAN; SPECTINOMYCIN; STREPTOMYCIN; TEICOPLANIN; VANCOMYCIN;

EID: 0033011933     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.12.3644-3648.1999     Document Type: Article
Times cited : (72)

References (37)
  • 1
    • 0345481253 scopus 로고    scopus 로고
    • Unpublished data
    • Arthur, M., et al. Unpublished data.
    • Arthur, M.1
  • 2
    • 0031735098 scopus 로고    scopus 로고
    • Requirement of the VanY and VanX D,D-peptidases for glycopeptide resistance in enterococci
    • Arthur, M., F. Depardieu, L. Cabanié, P. Reynolds, and P. Courvalin. 1998. Requirement of the VanY and VanX D,D-peptidases for glycopeptide resistance in enterococci. Mol. Microbiol. 31:819-830.
    • (1998) Mol. Microbiol. , vol.31 , pp. 819-830
    • Arthur, M.1    Depardieu, F.2    Cabanié, L.3    Reynolds, P.4    Courvalin, P.5
  • 3
    • 0031026581 scopus 로고    scopus 로고
    • The VanS sensor negatively controls VanR-mediated transcriptional activation of glycopeptide resistance genes of Tn1546 and related elements in the absence of induction
    • Arthur, M., F. Depardieu, G. Gerbaud, M. Galimand, R. Leclercq, and P. Courvalin. 1997. The VanS sensor negatively controls VanR-mediated transcriptional activation of glycopeptide resistance genes of Tn1546 and related elements in the absence of induction. J. Bacteriol. 179:97-106.
    • (1997) J. Bacteriol. , vol.179 , pp. 97-106
    • Arthur, M.1    Depardieu, F.2    Gerbaud, G.3    Galimand, M.4    Leclercq, R.5    Courvalin, P.6
  • 4
    • 0027941244 scopus 로고
    • Contribution of VanY DD-carboxypeptidase to grycopeptide resistance in Enterococcus faecalis by hydrolysis of peptidoglycan precursors
    • Arthur, M., F. Depardieu, H. A. Snaith, P. E. Reynolds, and P. Courvalin. 1994. Contribution of VanY DD-carboxypeptidase to grycopeptide resistance in Enterococcus faecalis by hydrolysis of peptidoglycan precursors. Antimicrob. Agents Chemother. 38:1899-1903.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1899-1903
    • Arthur, M.1    Depardieu, F.2    Snaith, H.A.3    Reynolds, P.E.4    Courvalin, P.5
  • 5
    • 0026697627 scopus 로고
    • Sequence of the vanY gene required for production of a vancomycin-inducible D,D-carboxypeptidase in Enterococcus faecium BM4147
    • Arthur, M., C. Molinas, and P. Courvalin. 1992. Sequence of the vanY gene required for production of a vancomycin-inducible D,D-carboxypeptidase in Enterococcus faecium BM4147. Gene 120:111-114.
    • (1992) Gene , vol.120 , pp. 111-114
    • Arthur, M.1    Molinas, C.2    Courvalin, P.3
  • 6
    • 0026658877 scopus 로고
    • The VanS-VanR two-component regulatory system controls synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147
    • Arthur, M., C. Molinas, and P. Courvalin. 1992. The VanS-VanR two-component regulatory system controls synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147. J. Bacteriol. 174:2582-2591.
    • (1992) J. Bacteriol. , vol.174 , pp. 2582-2591
    • Arthur, M.1    Molinas, C.2    Courvalin, P.3
  • 8
    • 0030796911 scopus 로고    scopus 로고
    • Mutations leading to increased levels of resistance to glycopeptide antibiotics in VanB-type enterococci
    • Baptista, M., F. Depardieu, P. Reynolds, P. Courvalin, and M. Arthur. 1997. Mutations leading to increased levels of resistance to glycopeptide antibiotics in VanB-type enterococci. Mol. Microbiol. 25:93-105.
    • (1997) Mol. Microbiol. , vol.25 , pp. 93-105
    • Baptista, M.1    Depardieu, F.2    Reynolds, P.3    Courvalin, P.4    Arthur, M.5
  • 9
    • 0028286852 scopus 로고
    • Modification of peptidoglycan precursors is a common feature of the low-level vancomycin-resistant VANB-type Enterococcus D366 and of the naturally glycopeptide-resistant species Lactobacillus casei, Pediococcus pentosaceus, Leuconostoc mesenteroides, and Enterococcus gallinarum
    • Billot-Klein, D., L. Gutmann, S. Sablé, E. Guittet, and J. van Heijenoort. 1994. Modification of peptidoglycan precursors is a common feature of the low-level vancomycin-resistant VANB-type Enterococcus D366 and of the naturally glycopeptide-resistant species Lactobacillus casei, Pediococcus pentosaceus, Leuconostoc mesenteroides, and Enterococcus gallinarum. J. Bacteriol. 176:2398-2405.
    • (1994) J. Bacteriol. , vol.176 , pp. 2398-2405
    • Billot-Klein, D.1    Gutmann, L.2    Sablé, S.3    Guittet, E.4    Van Heijenoort, J.5
  • 10
    • 0024296280 scopus 로고
    • Nucleotide sequences of the penicillin-binding protein 5 and 6 genes of Escherichia coli
    • Broome-Smith, J. K., I. Ioannidis, A. Edelman, and B. G. Spratt. 1988. Nucleotide sequences of the penicillin-binding protein 5 and 6 genes of Escherichia coli. Nucleic Acids Res. 16:1617.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 1617
    • Broome-Smith, J.K.1    Ioannidis, I.2    Edelman, A.3    Spratt, B.G.4
  • 11
    • 0026073599 scopus 로고
    • Identification of vancomycin resistance protein VanA as a D-alanine: D-alanine ligase of altered substrate specificity
    • Bugg, T. D. H., S. Dutka-Malen, M. Arthur, P. Courvalin, and C. T. Walsh. 1991. Identification of vancomycin resistance protein VanA as a D-alanine: D-alanine ligase of altered substrate specificity. Biochemistry 30:2017-2021.
    • (1991) Biochemistry , vol.30 , pp. 2017-2021
    • Bugg, T.D.H.1    Dutka-Malen, S.2    Arthur, M.3    Courvalin, P.4    Walsh, C.T.5
  • 12
    • 0026355435 scopus 로고
    • Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: Biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA
    • Bugg, T. D. H., G. D. Wright, S. Dutka-Malen, M. Arthur, P. Courvalin, and C. T. Walsh. 1991. Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA. Biochemistry 30:10408-10415.
    • (1991) Biochemistry , vol.30 , pp. 10408-10415
    • Bugg, T.D.H.1    Wright, G.D.2    Dutka-Malen, S.3    Arthur, M.4    Courvalin, P.5    Walsh, C.T.6
  • 13
    • 0021714276 scopus 로고
    • A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors
    • Churchward, G., D. Belin, and Y. Nagamine. 1984. A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors. Gene 31:165-171.
    • (1984) Gene , vol.31 , pp. 165-171
    • Churchward, G.1    Belin, D.2    Nagamine, Y.3
  • 14
    • 0029996927 scopus 로고    scopus 로고
    • Evolution of structure and substrate specificity in D-alanine: D-alanine ligases and related enzymes
    • Evers, S., B. Casadewall, M. Charles, S. Dutka-Malen, M. Galimand, and P. Courvalin. 1996. Evolution of structure and substrate specificity in D-alanine: D-alanine ligases and related enzymes. J. Mol. Evol. 42:706-712.
    • (1996) J. Mol. Evol. , vol.42 , pp. 706-712
    • Evers, S.1    Casadewall, B.2    Charles, M.3    Dutka-Malen, S.4    Galimand, M.5    Courvalin, P.6
  • 15
    • 0029863413 scopus 로고    scopus 로고
    • B two-component regulatory system in Enterococcus faecalis V583
    • B two-component regulatory system in Enterococcus faecalis V583. J. Bacteriol. 178:1302-1309.
    • (1996) J. Bacteriol. , vol.178 , pp. 1302-1309
    • Evers, S.1    Courvalin, P.2
  • 16
    • 0345049696 scopus 로고    scopus 로고
    • Unpublished data
    • Gholizadeh, Y., et al. Unpublished data.
    • Gholizadeh, Y.1
  • 17
    • 0032034821 scopus 로고    scopus 로고
    • Signal transduction in bacteria: Molecular mechanisms of stimulus-response coupling
    • Goudreau, P. N., and A. M. Stock. 1998. Signal transduction in bacteria: molecular mechanisms of stimulus-response coupling. Curr. Opin. Microbiol. 1:160-169.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 160-169
    • Goudreau, P.N.1    Stock, A.M.2
  • 18
    • 0023808730 scopus 로고
    • Plasmid-mediated resistance to vancomycin and teicoplanin in Enterococcus faecium
    • Leclercq, R., E. Derlot, J. Duval, and P. Courvalin. 1988. Plasmid-mediated resistance to vancomycin and teicoplanin in Enterococcus faecium. N. Engl. J. Med. 319:157-161.
    • (1988) N. Engl. J. Med. , vol.319 , pp. 157-161
    • Leclercq, R.1    Derlot, E.2    Duval, J.3    Courvalin, P.4
  • 19
    • 0030779872 scopus 로고    scopus 로고
    • Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX
    • McCafferty, D. G., I. A. Lessard, and C. T. Walsh. 1997. Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX. Biochemistry 36:10498-10505.
    • (1997) Biochemistry , vol.36 , pp. 10498-10505
    • McCafferty, D.G.1    Lessard, I.A.2    Walsh, C.T.3
  • 20
    • 0028149883 scopus 로고
    • Purification and characterization of the VanB ligase associated with type B vancomycin resistance in Enterococcus faecalis V583
    • Meziane-Cherif, D., M. A. Badet-Denisot, S. Evers, P. Courvalin, and B. Badet. 1994. Purification and characterization of the VanB ligase associated with type B vancomycin resistance in Enterococcus faecalis V583. FEBS Lett. 354:140-142.
    • (1994) FEBS Lett. , vol.354 , pp. 140-142
    • Meziane-Cherif, D.1    Badet-Denisot, M.A.2    Evers, S.3    Courvalin, P.4    Badet, B.5
  • 23
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson, J., and E. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:71-112.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.1    Kofoid, E.2
  • 25
    • 0024355483 scopus 로고
    • Structure, biochemistry and mechanism of action of glycopeptide antibiotics
    • Reynolds, P. E. 1989. Structure, biochemistry and mechanism of action of glycopeptide antibiotics. Eur. J. Clin. Microbiol. Infect. Dis. 8:943-950.
    • (1989) Eur. J. Clin. Microbiol. Infect. Dis. , vol.8 , pp. 943-950
    • Reynolds, P.E.1
  • 26
    • 0028076784 scopus 로고
    • Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine
    • Reynolds, P. E., F. Depardieu, S. Dutka-Malen, M. Arthur, and P. Courvalin. 1994. Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine. Mol. Microbiol. 13:1065-1070.
    • (1994) Mol. Microbiol. , vol.13 , pp. 1065-1070
    • Reynolds, P.E.1    Depardieu, F.2    Dutka-Malen, S.3    Arthur, M.4    Courvalin, P.5
  • 27
    • 0028932504 scopus 로고
    • Inducible and constitutive expression of resistance to glycopeptides and vancomycin dependence in glycopeptide-resistant Enterococcus avium
    • Rosato, A., J. Pierre, D. Billot-Klein, A. Buu-Hoi, and L. Gutmann. 1995. Inducible and constitutive expression of resistance to glycopeptides and vancomycin dependence in glycopeptide-resistant Enterococcus avium. Antimicrob. Agents Chemother. 39:830-833.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 830-833
    • Rosato, A.1    Pierre, J.2    Billot-Klein, D.3    Buu-Hoi, A.4    Gutmann, L.5
  • 30
    • 0029189932 scopus 로고
    • Electroporation and efficient transformation of Enterococcus faecalis grown in high concentrations of glycine
    • Shepard, B. D., and M. S. Gilmore. 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
  • 31
    • 0031009298 scopus 로고    scopus 로고
    • Vancomycin dependence in a VanA-producing Enterococcus avium strain with a nonsense mutation in the natural D-Ala-D-Ala ligase gene
    • Sifaoui, F., and L. Gutmann. 1997. Vancomycin dependence in a VanA-producing Enterococcus avium strain with a nonsense mutation in the natural D-Ala-D-Ala ligase gene. Antimicrob. Agents Chemother. 41:1409.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1409
    • Sifaoui, F.1    Gutmann, L.2
  • 32
    • 84924083068 scopus 로고
    • An inocula replicating apparatus for routine testing of bacterial susceptibility to antibiotics
    • Steers, E., E. L. Foltz, B. S. Graves, and J. Rindel. 1959. An inocula replicating apparatus for routine testing of bacterial susceptibility to antibiotics. Antibiot. Chemother. (Basel) 9:307-311.
    • (1959) Antibiot. Chemother. (Basel) , vol.9 , pp. 307-311
    • Steers, E.1    Foltz, E.L.2    Graves, B.S.3    Rindel, J.4
  • 33
    • 0030584680 scopus 로고    scopus 로고
    • Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase
    • Stoll, V. S., M. S. Kimber, and E. F. Pai. 1996. Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase. Structure 4:437-447.
    • (1996) Structure , vol.4 , pp. 437-447
    • Stoll, V.S.1    Kimber, M.S.2    Pai, E.F.3
  • 35
    • 0020442864 scopus 로고
    • The pUC plasmids and M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieira, J., and J. Messing. 1982. The pUC plasmids and M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19:259-268.
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 36
    • 0026634121 scopus 로고
    • Characterization of a Bacillus subtilis sporulation operon that includes genes for an RNA polymerase σ factor and for a putative DD-carboxypeptidase
    • Wu, J.-J., R. Schuch, and P. J. Piggot 1992. Characterization of a Bacillus subtilis sporulation operon that includes genes for an RNA polymerase σ factor and for a putative DD-carboxypeptidase. J. Bacteriol. 174:4885-4892.
    • (1992) J. Bacteriol. , vol.174 , pp. 4885-4892
    • Wu, J.-J.1    Schuch, R.2    Piggot, P.J.3
  • 37
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.