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Volumn 43, Issue 8, 1999, Pages 1875-1880

Moderate-level resistance to glycopeptide LY333328 mediated by genes of the vanA and vanB clusters in enterococci

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPEPTIDE; ORITAVANCIN; TEICOPLANIN;

EID: 0032818228     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.43.8.1875     Document Type: Article
Times cited : (65)

References (36)
  • 1
    • 0029797308 scopus 로고    scopus 로고
    • Inhibition of peptidoglycan biosynthesis in vancomycin-susceptible and -resistant bacteria by a semi-synthetic glycopeptide antibiotic
    • Allen, N. E., J. N. Hobbs, Jr., and T. I. Nicas. 1996. Inhibition of peptidoglycan biosynthesis in vancomycin-susceptible and -resistant bacteria by a semi-synthetic glycopeptide antibiotic. Antimicrob. Agents Chemother. 40:2356-2362.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 2356-2362
    • Allen, N.E.1    Hobbs J.N., Jr.2    Nicas, T.I.3
  • 2
    • 0031038392 scopus 로고    scopus 로고
    • Molecular interactions of a semisynthetic glycopeptide antibiotic with D-alanyl-D-alanine and D-alanyl-D-lactate residues
    • Allen, N. E., D. L. LeTourneau, and J. N. Hobbs, Jr. 1997. Molecular interactions of a semisynthetic glycopeptide antibiotic with D-alanyl-D-alanine and D-alanyl-D-lactate residues. Antimicrob. Agents Chermother. 41:66-71.
    • (1997) Antimicrob. Agents Chermother. , vol.41 , pp. 66-71
    • Allen, N.E.1    LeTourneau, D.L.2    Hobbs J.N., Jr.3
  • 3
    • 0027266017 scopus 로고
    • Genetics and mechanisms of glycopeptide resistance in enterococci
    • Arthur, M., and P. Courvalin. 1993. Genetics and mechanisms of glycopeptide resistance in enterococci. Antimicrob. Agents Chemother. 37:1563-1571.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 1563-1571
    • Arthur, M.1    Courvalin, P.2
  • 4
    • 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. 30:819-830.
    • (1998) Mol. Microbiol. , vol.30 , pp. 819-830
    • Arthur, M.1    Depardieu, F.2    Cabanié, L.3    Reynolds, P.4    Courvalin, P.5
  • 5
    • 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
  • 6
    • 0028870094 scopus 로고
    • The vanZ gene of Tn1546 from Enterococcus faecium BM4147 confers resistance to teicoplanin
    • Arthur, M., F. Depardieu, C. Molinas, P. Reynolds, and P. Courvalin. 1995. The vanZ gene of Tn1546 from Enterococcus faecium BM4147 confers resistance to teicoplanin. Gene 154:87-92.
    • (1995) Gene , vol.154 , pp. 87-92
    • Arthur, M.1    Depardieu, F.2    Molinas, C.3    Reynolds, P.4    Courvalin, P.5
  • 7
    • 0030036676 scopus 로고    scopus 로고
    • Quantitative analysis of the metabolism of soluble cytoplasmic peptidoglycan precursors of glycopeptide-resistant enterococci
    • Arthur, M., F. Depardieu, P. Reynolds, and P. Courvalin. 1996. Quantitative analysis of the metabolism of soluble cytoplasmic peptidoglycan precursors of glycopeptide-resistant enterococci. Mol. Microbiol. 21:33-44.
    • (1996) Mol. Microbiol. , vol.21 , pp. 33-44
    • Arthur, M.1    Depardieu, F.2    Reynolds, P.3    Courvalin, P.4
  • 8
    • 0027941244 scopus 로고
    • Contribution of VanY D,D-carboxypeptidase to glycopeptide 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 D,D-carboxypeptidase to glycopeptide 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
  • 9
    • 0026506576 scopus 로고
    • Evidence for in vivo incorporation of D-lactate into peptidoglycan precursors of vancomycin-resistant enterococci
    • Arthur, M., C. Molinas, T. D. H. Bugg, G. D. Wright, C. T. Walsh, and P. Courvalin. 1992. Evidence for in vivo incorporation of D-lactate into peptidoglycan precursors of vancomycin-resistant enterococci. Antimicrob. Agents Chemother. 34:867-869.
    • (1992) Antimicrob. Agents Chemother. , vol.34 , pp. 867-869
    • Arthur, M.1    Molinas, C.2    Bugg, T.D.H.3    Wright, G.D.4    Walsh, C.T.5    Courvalin, P.6
  • 10
    • 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
  • 12
    • 0031017889 scopus 로고    scopus 로고
    • Selection of glycopeptide-resistant mutants of VanB-type Enterococcus faecalis BM4281 in vitro and in experimental endocarditis
    • Aslangul, E., M. Baptista, B. Fantin, F. Depardieu, M. Arthur, P. Courvalin, and C. Carbon. 1997. Selection of glycopeptide-resistant mutants of VanB-type Enterococcus faecalis BM4281 in vitro and in experimental endocarditis. J. Infect. Dis. 175:598-605.
    • (1997) J. Infect. Dis. , vol.175 , pp. 598-605
    • Aslangul, E.1    Baptista, M.2    Fantin, B.3    Depardieu, F.4    Arthur, M.5    Courvalin, P.6    Carbon, C.7
  • 13
    • 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
  • 14
    • 0021154432 scopus 로고
    • The structure and mode of action of glycopeptide antibiotics of the vancomycin group
    • Barna, J. C. J., and D. H. Williams. 1984. The structure and mode of action of glycopeptide antibiotics of the vancomycin group. Annu. Rev. Microbiol. 38:339-357.
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 339-357
    • Barna, J.C.J.1    Williams, D.H.2
  • 15
    • 0030717475 scopus 로고    scopus 로고
    • Semiquantitation of cooperatively in binding of vancomycin-group antibiotics to vancomycin-susceptible and -resistant organisms
    • Beauregard, D., A. Maguire, D. Williams, and P. Reynolds. 1997. Semiquantitation of cooperatively in binding of vancomycin-group antibiotics to vancomycin-susceptible and -resistant organisms. Antimicrob. Agents Chemother. 41:2418-2423.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 2418-2423
    • Beauregard, D.1    Maguire, A.2    Williams, D.3    Reynolds, P.4
  • 17
    • 0028605482 scopus 로고
    • Association constants for the binding of vancomycin and teicoplanin to N-acetyl-D-alanyl-D-alanine and N-acetyl-D-alanyl-D-serine
    • Billot-Klein, D., D. Blanot, L. Gutmann, and J. van Heijenoort. 1994. Association constants for the binding of vancomycin and teicoplanin to N-acetyl-D-alanyl-D-alanine and N-acetyl-D-alanyl-D-serine. Biochem. J. 304: 1021-1022.
    • (1994) Biochem. J. , vol.304 , pp. 1021-1022
    • Billot-Klein, D.1    Blanot, D.2    Gutmann, L.3    Van Heijenoort, J.4
  • 18
    • 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
  • 19
    • 0030899624 scopus 로고    scopus 로고
    • N-alkyl-substituted glycopeptide antibiotics
    • Chopra, I. 1997. N-alkyl-substituted glycopeptide antibiotics. Exp. Opin. Investig. Drugs 6:299-303.
    • (1997) Exp. Opin. Investig. Drugs , vol.6 , pp. 299-303
    • Chopra, I.1
  • 20
    • 0022898196 scopus 로고
    • Transposable multiple antibiotic resistance in Streptococcus pneumoniae
    • Courvalin, P., and C. Carlier. 1986. Transposable multiple antibiotic resistance in Streptococcus pneumoniae. Mol. Gen. Genet. 205:291-297.
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 291-297
    • Courvalin, P.1    Carlier, C.2
  • 21
    • 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
  • 22
    • 0028587626 scopus 로고
    • Urinary tract infection with an Enterococcus faecalis isolate that requires vancomycin for growth
    • Fraimow, H. S., D. L. Jungkind, D. W. Lander, D. R. Delso, and J. L. Dean. 1994. Urinary tract infection with an Enterococcus faecalis isolate that requires vancomycin for growth. Ann. Intern. Med. 121:22-26.
    • (1994) Ann. Intern. Med. , vol.121 , pp. 22-26
    • Fraimow, H.S.1    Jungkind, D.L.2    Lander, D.W.3    Delso, D.R.4    Dean, J.L.5
  • 24
    • 0027534597 scopus 로고
    • In vivo development of teicoplanin resistance in a VanB Enterococcus faecium isolate
    • Hayden, M. K., G. M. Trenholme, J. E. Schultz, and D. F. Sahm. 1993. In vivo development of teicoplanin resistance in a VanB Enterococcus faecium isolate. J. Infect. Dis. 167:1224-1227.
    • (1993) J. Infect. Dis. , vol.167 , pp. 1224-1227
    • Hayden, M.K.1    Trenholme, G.M.2    Schultz, J.E.3    Sahm, D.F.4
  • 25
    • 0015980566 scopus 로고
    • Conjugal transfer of plasmid-borne multiple antibiotic resistance in Streptococcus faecalis var, zymogenes
    • Jacob, A. E., and S. J. Hobbs. 1974. Conjugal transfer of plasmid-borne multiple antibiotic resistance in Streptococcus faecalis var, zymogenes. J. Bacteriol. 117:360-372.
    • (1974) J. Bacteriol. , vol.117 , pp. 360-372
    • Jacob, A.E.1    Hobbs, S.J.2
  • 26
    • 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
  • 27
    • 0026892270 scopus 로고
    • Modified peptidoglycan precursors produced by glycopeptide-resistant enterococci
    • Messer, J., and P. E. Reynolds. 1992. Modified peptidoglycan precursors produced by glycopeptide-resistant enterococci. FEMS Microbiol. Lett. 94: 195-200.
    • (1992) FEMS Microbiol. Lett. , vol.94 , pp. 195-200
    • Messer, J.1    Reynolds, P.E.2
  • 28
    • 0030751187 scopus 로고    scopus 로고
    • Beyond vancomycin: New therapies to meet the challenge of glycopeptide resistance
    • Nicas, T., M. Zeckel, and D. Braun. 1997. Beyond vancomycin: new therapies to meet the challenge of glycopeptide resistance. Trends Microbiol. 5:240-249.
    • (1997) Trends Microbiol. , vol.5 , pp. 240-249
    • Nicas, T.1    Zeckel, M.2    Braun, D.3
  • 29
    • 0015102039 scopus 로고
    • Modifications of the acyl-D-alanyl-D-alanine terminus affecting complex-formation with vancomycin
    • Nieto, M., and H. R. Perkins. 1971. Modifications of the acyl-D-alanyl-D-alanine terminus affecting complex-formation with vancomycin. Biochem. J. 123:789-803.
    • (1971) Biochem. J. , vol.123 , pp. 789-803
    • Nieto, M.1    Perkins, H.R.2
  • 30
    • 0029889580 scopus 로고    scopus 로고
    • Characterization of Tn1547, a composite transposon flanked by the IS16 and IS256-like elements, that confers vancomycin resistance in Enterococcus faecalis BM4281
    • Quintiliani, R., Jr., and P. Courvalin. 1996. Characterization of Tn1547, a composite transposon flanked by the IS16 and IS256-like elements, that confers vancomycin resistance in Enterococcus faecalis BM4281. Gene 172: 1-8.
    • (1996) Gene , vol.172 , pp. 1-8
    • Quintiliani R., Jr.1    Courvalin, P.2
  • 31
    • 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. Bun-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    Bun-Hoi, A.4    Gutmann, L.5
  • 33
    • 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. Riden. 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    Riden, J.4
  • 35
    • 0000437775 scopus 로고
    • D-Alanyl-D-alanine ligases and the molecular mechanism of vancomycin resistance
    • Wright G. D., and C. T. Walsh. 1992. D-Alanyl-D-alanine ligases and the molecular mechanism of vancomycin resistance. Acc. Chem. Res. 25:468-473.
    • (1992) Acc. Chem. Res. , vol.25 , pp. 468-473
    • Wright, G.D.1    Walsh, C.T.2
  • 36
    • 0033020091 scopus 로고    scopus 로고
    • Synergy of an investigational glycopeptide, LY333328, with once-daily gentamicin against vancomycin-resistant Enterococcus faecium in a multiple-dose, in vitro pharmacodynamic model
    • Zelenitsky, S. A., B. Booker, N. Laing, J. A. Karlowsky, D. J. Hoban, and G. G. Zhanel. 1999. Synergy of an investigational glycopeptide, LY333328, with once-daily gentamicin against vancomycin-resistant Enterococcus faecium in a multiple-dose, in vitro pharmacodynamic model. Antimicrob. Agents Chemother. 43:592-597.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 592-597
    • Zelenitsky, S.A.1    Booker, B.2    Laing, N.3    Karlowsky, J.A.4    Hoban, D.J.5    Zhanel, G.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.