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Volumn 42, Issue 9, 1998, Pages 2215-2220

Glycopeptide antibiotic resistance genes in glycopeptide-producing organisms

Author keywords

[No Author keywords available]

Indexed keywords

A47934; GLYCOPEPTIDE; UNCLASSIFIED DRUG; VANCOMYCIN;

EID: 0031663280     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.42.9.2215     Document Type: Article
Times cited : (195)

References (44)
  • 1
    • 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
  • 2
    • 0027391961 scopus 로고
    • Characterization of Tn1546, a Tn3-related transposon conferring glycopeptide resistance by synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147
    • Arthur, M., C. Molinas, F. Depardieu, and P. Courvalin. 1993. Characterization of Tn1546, a Tn3-related transposon conferring glycopeptide resistance by synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147. J. Bacteriol. 175:117-127.
    • (1993) J. Bacteriol. , vol.175 , pp. 117-127
    • Arthur, M.1    Molinas, C.2    Depardieu, F.3    Courvalin, P.4
  • 3
    • 0025741584 scopus 로고
    • Structural relationship between the vancomycin resistance protein VanH and 2-hydroxycarboxylic acid dehydrogenases
    • Arthur, M., C. Molinas, S. Dutka-Malen, and P. Courvalin. 1991. Structural relationship between the vancomycin resistance protein VanH and 2-hydroxycarboxylic acid dehydrogenases. Gene 103:133-134.
    • (1991) Gene , vol.103 , pp. 133-134
    • Arthur, M.1    Molinas, C.2    Dutka-Malen, S.3    Courvalin, P.4
  • 5
    • 0031178855 scopus 로고    scopus 로고
    • Avoparcin used as a growth promoter is associated with the occurrence of vancomycin-resistant Enterococcus faecium on Danish poultry and pig farms
    • Bager, F., M. Madsen, J. Christensen, and F. M. Aarestrup. 1997. Avoparcin used as a growth promoter is associated with the occurrence of vancomycin-resistant Enterococcus faecium on Danish poultry and pig farms. Prev. Vet. Med. 31:95-112.
    • (1997) Prev. Vet. Med. , vol.31 , pp. 95-112
    • Bager, F.1    Madsen, M.2    Christensen, J.3    Aarestrup, F.M.4
  • 6
    • 0021154432 scopus 로고
    • The structure and mode of action of glycopeptide antibiotics
    • Barna, J. C. J., and D. H. Williams. 1984. The structure and mode of action of glycopeptide antibiotics. Annu. Rev. Microbiol. 38:339-357.
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 339-357
    • Barna, J.C.J.1    Williams, D.H.2
  • 7
    • 0028149741 scopus 로고
    • Farm animals as a putative reservoir for vancomycin-resistant enterococcal infection in man
    • Bates, J., J. Z. Jordens, and D. T. Griffiths. 1994. Farm animals as a putative reservoir for vancomycin-resistant enterococcal infection in man. J. Antimicrob. Chemother. 34:507-516.
    • (1994) J. Antimicrob. Chemother. , vol.34 , pp. 507-516
    • Bates, J.1    Jordens, J.Z.2    Griffiths, D.T.3
  • 8
    • 0021710537 scopus 로고
    • The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences
    • Bibb, M. J., P. R. Findlay, and M. W. Johnson. 1984. The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences. Gene 30:157-166.
    • (1984) Gene , vol.30 , pp. 157-166
    • Bibb, M.J.1    Findlay, P.R.2    Johnson, M.W.3
  • 9
    • 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
  • 10
    • 0029956752 scopus 로고    scopus 로고
    • Vancomycin-resistant enterococci from nosocomial, community, and animal sources in the United States
    • Coque, T. M., J. F. Tomayko, S. C. Ricke, P. C. Okhyusen, and B. E. Murray. 1996. Vancomycin-resistant enterococci from nosocomial, community, and animal sources in the United States. Antimicrob. Agents Chemother. 40: 2605-2609.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 2605-2609
    • Coque, T.M.1    Tomayko, J.F.2    Ricke, S.C.3    Okhyusen, P.C.4    Murray, B.E.5
  • 12
    • 0029025525 scopus 로고
    • Purification, properties and DNA sequence of the D-lactate dehydrogenase from Leuconostoc mesenteroides subsp. cremoris
    • Dartois, V., V. Phalip, P. Schmitt, and C. Divies. 1995. Purification, properties and DNA sequence of the D-lactate dehydrogenase from Leuconostoc mesenteroides subsp. cremoris. Res. Microbiol. 146:291-302.
    • (1995) Res. Microbiol. , vol.146 , pp. 291-302
    • Dartois, V.1    Phalip, V.2    Schmitt, P.3    Divies, C.4
  • 14
    • 0026522234 scopus 로고
    • Sequence of the vanC gene of Enterococcus gallinarum BM4174 encoding a D-alanine: D-alanine ligase-related protein necessary for vancomycin resistance
    • Dutka-Malen, S., C. Molinas, M. Arthur, and P. Courvalin. 1992. Sequence of the vanC gene of Enterococcus gallinarum BM4174 encoding a D-alanine: D-alanine ligase-related protein necessary for vancomycin resistance. Gene 112:53-58.
    • (1992) Gene , vol.112 , pp. 53-58
    • Dutka-Malen, S.1    Molinas, C.2    Arthur, M.3    Courvalin, P.4
  • 15
    • 0028982632 scopus 로고
    • Analysis of genes encoding D-alanine: D-alanine ligase-related enzymes in Leuconostoc mesenteroides and Lactobacillus spp
    • Elisha, B. G., and P. Courvalin. 1995. Analysis of genes encoding D-alanine: D-alanine ligase-related enzymes in Leuconostoc mesenteroides and Lactobacillus spp. Gene 152:79-83.
    • (1995) Gene , vol.152 , pp. 79-83
    • Elisha, B.G.1    Courvalin, P.2
  • 16
    • 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
  • 17
    • 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
  • 18
    • 0027518660 scopus 로고
    • The vanB gene of vancomycin-resistant Enterococcus faecalis V583 is structurally related to genes encoding D-Ala:D-Ala ligases and glycopeptide-resistance proteins VanA and VanC
    • Evers, S., D. F. Sahm, and P. Courvalin. 1993. The vanB gene of vancomycin-resistant Enterococcus faecalis V583 is structurally related to genes encoding D-Ala:D-Ala ligases and glycopeptide-resistance proteins VanA and VanC. Gene 124:143-144.
    • (1993) Gene , vol.124 , pp. 143-144
    • Evers, S.1    Sahm, D.F.2    Courvalin, P.3
  • 19
  • 21
    • 0026713575 scopus 로고
    • Glutamate 264 modulates the pH dependence of the NAD(+)-dependent D-lactate dehydrogenase
    • Kochhar, S., N. Chuard, and H. Hottinger. 1992. Glutamate 264 modulates the pH dependence of the NAD(+)-dependent D-lactate dehydrogenase. J. Biol. Chem. 267:20298-20301.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20298-20301
    • Kochhar, S.1    Chuard, N.2    Hottinger, H.3
  • 22
    • 0030903151 scopus 로고    scopus 로고
    • Resistance to glycopeptides in enterococci
    • Leclercq, R., and P. Courvalin. 1997. Resistance to glycopeptides in enterococci. Clin. Infect. Dis. 24:545-554.
    • (1997) Clin. Infect. Dis. , vol.24 , pp. 545-554
    • Leclercq, R.1    Courvalin, P.2
  • 23
    • 0030911603 scopus 로고    scopus 로고
    • D-AlaD-Ala ligases from glycopeptide antibiotic-producing organisms are highly homologous to the enterococcal vancomycin-resistance ligases VanA and VanB
    • Marshall, C. G., G. Broadhead, B. Leskiw, and G. D. Wright. 1997. D-AlaD-Ala ligases from glycopeptide antibiotic-producing organisms are highly homologous to the enterococcal vancomycin-resistance ligases VanA and VanB Proc Natl. Acad. Sci. USA 94:6480-6483.
    • (1997) Proc Natl. Acad. Sci. USA , vol.94 , pp. 6480-6483
    • Marshall, C.G.1    Broadhead, G.2    Leskiw, B.3    Wright, G.D.4
  • 24
    • 0031573771 scopus 로고    scopus 로고
    • The glycopeptide antibiotic producer Streptomyces toyocaensis NRRL 15009 has both D-alanyl-D-alanine and D-alanyl-D-lactate ligases
    • Marshall, C. G., and G. D. Wright. 1997. The glycopeptide antibiotic producer Streptomyces toyocaensis NRRL 15009 has both D-alanyl-D-alanine and D-alanyl-D-lactate ligases. FEMS Microbiol. Lett. 157:295-299.
    • (1997) FEMS Microbiol. Lett. , vol.157 , pp. 295-299
    • Marshall, C.G.1    Wright, G.D.2
  • 25
    • 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
  • 26
    • 0031178966 scopus 로고    scopus 로고
    • Vancomycin-resistant enterococci outside the health-care setting: Prevalence, sources, and public health implications
    • McDonald, L. C., M. J. Kuehnert, F. C. Tenover, and W. R. Jarvis. 1997. Vancomycin-resistant enterococci outside the health-care setting: prevalence, sources, and public health implications. Emerg. Infect. Dis. 3:311-317.
    • (1997) Emerg. Infect. Dis. , vol.3 , pp. 311-317
    • McDonald, L.C.1    Kuehnert, M.J.2    Tenover, F.C.3    Jarvis, W.R.4
  • 27
    • 0030913158 scopus 로고    scopus 로고
    • Vancomycin-resistant enterococci
    • Murray, E. 1997. Vancomycin-resistant enterococci. Am. J. Med. 102:284-293.
    • (1997) Am. J. Med. , vol.102 , pp. 284-293
    • Murray, E.1
  • 28
    • 0030922878 scopus 로고    scopus 로고
    • Bacterial resistance to vancomycin: Overproduction, purification, and characterization of VanC2 from Enterococcus casseliflavus as a D-Ala-D-Ser ligase
    • Park, I. S., C. H. Lin, and C. T. Walsh. 1997. Bacterial resistance to vancomycin: overproduction, purification, and characterization of VanC2 from Enterococcus casseliflavus as a D-Ala-D-Ser ligase. Proc. Natl. Acad. Sci. USA 94:10040-10044.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10040-10044
    • Park, I.S.1    Lin, C.H.2    Walsh, C.T.3
  • 29
    • 0030960777 scopus 로고    scopus 로고
    • D-Alanyl-D-lactate and D-alanyl-D-alanine synthesis by D-alanyl-D-alanine ligase from vancomycin-resistant Leuconostoc mesenteroides. Effects of a phenylalanine 261 to tyrosine mutation
    • Park, I. S., and C. T. Walsh. 1997. D-Alanyl-D-lactate and D-alanyl-D-alanine synthesis by D-alanyl-D-alanine ligase from vancomycin-resistant Leuconostoc mesenteroides. Effects of a phenylalanine 261 to tyrosine mutation. J. Biol. Chem. 272:9210-9214.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9210-9214
    • Park, I.S.1    Walsh, C.T.2
  • 30
    • 0028825954 scopus 로고
    • VanA genes in vancomycin-resistant clinical isolates of Oerskovia turbata and Arcanobacterium (Cornebacterium) haemolyticum
    • Power, E. G. M., Y. H. Abdulla, H. G. Talsania, W. Spice, S. Aathithan, and G. L. French. 1995. VanA genes in vancomycin-resistant clinical isolates of Oerskovia turbata and Arcanobacterium (Cornebacterium) haemolyticum. J. Antimicrob. Chemother. 36:595-606.
    • (1995) J. Antimicrob. Chemother. , vol.36 , pp. 595-606
    • Power, E.G.M.1    Abdulla, Y.H.2    Talsania, H.G.3    Spice, W.4    Aathithan, S.5    French, G.L.6
  • 31
    • 0029889580 scopus 로고    scopus 로고
    • Characterization of Tn1547, a composite transposon flanked by the IS16 and IS256-like elements, that confers vancomycin resistance in Enterococus faecalis BM428
    • Quintiliani, R. J., and P. Courvalin. 1996. Characterization of Tn1547, a composite transposon flanked by the IS16 and IS256-like elements, that confers vancomycin resistance in Enterococus faecalis BM428. Gene 172: 1-8.
    • (1996) Gene , vol.172 , pp. 1-8
    • Quintiliani, R.J.1    Courvalin, P.2
  • 32
    • 0028178947 scopus 로고
    • Conjugal transfer of the vancomycin resistance determinant vanB between enterococci involves the movement of large genetic elements from chromosome to chromosome
    • Quintiliani, R. J., and P. Courvalin. 1994. Conjugal transfer of the vancomycin resistance determinant vanB between enterococci involves the movement of large genetic elements from chromosome to chromosome. FEMS Microbiol. Lett. 119:359-363.
    • (1994) FEMS Microbiol. Lett. , vol.119 , pp. 359-363
    • Quintiliani, R.J.1    Courvalin, P.2
  • 33
    • 0027405032 scopus 로고
    • The vanB gene confers various levels of self-transferable resistance to vancomycin in enterococci
    • Quintiliani, R. J., S. Evers, and P. Courvalin. 1993. The vanB gene confers various levels of self-transferable resistance to vancomycin in enterococci. J. Infect. Dis. 167:1220-1223.
    • (1993) J. Infect. Dis. , vol.167 , pp. 1220-1223
    • Quintiliani, R.J.1    Evers, S.2    Courvalin, P.3
  • 34
    • 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
  • 35
    • 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
  • 36
    • 0026549146 scopus 로고
    • Compilation and analysis of DNA sequences associated with apparent streptomycete promoters
    • Strohl, W. R. 1992. Compilation and analysis of DNA sequences associated with apparent streptomycete promoters. Nucleic Acids Res. 20:961-974.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 961-974
    • Strohl, W.R.1
  • 37
    • 0028361499 scopus 로고
    • Essential role of arginine 235 in the substrate-binding of Lactobacillus plantarum D-lactate dehydrogenase
    • Taguchi, H., and T. Ohta. 1994. Essential role of arginine 235 in the substrate-binding of Lactobacillus plantarum D-lactate dehydrogenase. J. Biochem. 115:930-936.
    • (1994) J. Biochem. , vol.115 , pp. 930-936
    • Taguchi, H.1    Ohta, T.2
  • 38
    • 0027323970 scopus 로고
    • Histidine 296 is essential for the catalysis in Lactobacillus plantarum D-lactate dehydrogenase
    • Taguchi, H., and T. Ohta. 1993. Histidine 296 is essential for the catalysis in Lactobacillus plantarum D-lactate dehydrogenase. J. Biol. Chem. 268:18030-18034.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18030-18034
    • Taguchi, H.1    Ohta, T.2
  • 39
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 40
    • 0029678259 scopus 로고    scopus 로고
    • Bacterial resistance to vancomycin: Five genes and one missing hydrogen bond tell the story
    • Walsh, C. T., S. L. Fisher, L.-S. Park, M. Prahalad, and Z. Wu. 1996. Bacterial resistance to vancomycin: five genes and one missing hydrogen bond tell the story. Chem. Biol. 3:21-28.
    • (1996) Chem. Biol. , vol.3 , pp. 21-28
    • Walsh, C.T.1    Fisher, S.L.2    Park, L.-S.3    Prahalad, M.4    Wu, Z.5
  • 41
    • 0027496523 scopus 로고
    • Antibiotic preparations contain DNA: A source of drug resistance genes?
    • Webb, V., and J. Davies. 1993. Antibiotic preparations contain DNA: a source of drug resistance genes? Antimicrob. Agents Chemother. 37:2379-2384.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 2379-2384
    • Webb, V.1    Davies, J.2
  • 42
    • 0028910817 scopus 로고
    • Linkage of vancomycin and high-level gentamicin resistance genes on the same plasmid in a clinical isolate of Enterococcus faecalis
    • Woodford, N., B. L. Jones, Z. Baccus, H. A. Ludlam, and D. F. Brown. 1995. Linkage of vancomycin and high-level gentamicin resistance genes on the same plasmid in a clinical isolate of Enterococcus faecalis. J. Antimicrob. Chemother. 35:179-184.
    • (1995) J. Antimicrob. Chemother. , vol.35 , pp. 179-184
    • Woodford, N.1    Jones, B.L.2    Baccus, Z.3    Ludlam, H.A.4    Brown, D.F.5
  • 43
    • 0028959077 scopus 로고
    • Overexpression, purification, and characterization of VanX, a D,D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147
    • Wu, Z., G. D. Wright, and C. T. Walsh. 1995. Overexpression, purification, and characterization of VanX, a D,D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147. Biochemistry 34:2455-2463.
    • (1995) Biochemistry , vol.34 , pp. 2455-2463
    • Wu, Z.1    Wright, G.D.2    Walsh, C.T.3


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