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Volumn 48, Issue 4, 2004, Pages 314-319

Increasing vancomycin susceptibility in vancomycin resistant enterococci by vanH promoter and ddl transformation

Author keywords

Bacteria; Enterococcus; Transformation; Vancomycin; Vancomycin resistance

Indexed keywords

PLASMID DNA; VANCOMYCIN;

EID: 1942505921     PISSN: 01634453     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jinf.2003.10.017     Document Type: Article
Times cited : (2)

References (25)
  • 1
    • 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, Molinas C, Depardieu F, Courvalin P. Characterization of Tn1546, a Tn3-related transposon conferring glycopeptide resistance by synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147. J Bacteriol 1993;175:117-127.
    • (1993) J. Bacteriol. , vol.175 , pp. 117-127
    • Arthur, M.1    Molinas, C.2    Depardieu, F.3    Courvalin, P.4
  • 2
    • 0025674740 scopus 로고
    • Resistance of enterococci to glycopeptides
    • Courvalin P. Resistance of enterococci to glycopeptides. Antimicrob Agents Chemother 1990;34:2291-2296.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 2291-2296
    • Courvalin, P.1
  • 3
    • 16144367104 scopus 로고    scopus 로고
    • Preparing for battle against vancomycin resistance (News)
    • Rowe PM. Preparing for battle against vancomycin resistance (News). Lancet 1996;347:252.
    • (1996) Lancet , vol.347 , pp. 252
    • Rowe, P.M.1
  • 4
    • 0023808730 scopus 로고    scopus 로고
    • Plasmid mediated resistance to vancomycin and teicoplanin in Enterococcus faecium
    • Lecklercq R, Derlot E, Duval J, Courvalin P. Plasmid mediated resistance to vancomycin and teicoplanin in Enterococcus faecium. N Engl J Med 1998;319:157-161.
    • (1998) N. Engl. J. Med. , vol.319 , pp. 157-161
    • Lecklercq, R.1    Derlot, E.2    Duval, J.3    Courvalin, P.4
  • 6
    • 2442756432 scopus 로고    scopus 로고
    • Vancomycin resistant enterococcal infections in Korea
    • Kim JM, Song YG. Vancomycin resistant enterococcal infections in Korea. Yonsei Med J 1998;39:562-568.
    • (1998) Yonsei Med. J. , vol.39 , pp. 562-568
    • Kim, J.M.1    Song, Y.G.2
  • 8
    • 0034680167 scopus 로고    scopus 로고
    • Molecular mechanisms that confer antibacterial drug resistance
    • Walsh C. Molecular mechanisms that confer antibacterial drug resistance. Nature 2000;406:775-781.
    • (2000) Nature , vol.406 , pp. 775-781
    • Walsh, C.1
  • 9
    • 0029678259 scopus 로고    scopus 로고
    • Bacterial resistance to vancomycin: Five genes and one missing hydrogen bond tell the story
    • Walsh C, Fisher SL, Park IS, Prahald M, Wu Z. Bacterial resistance to vancomycin: five genes and one missing hydrogen bond tell the story. Chem Biol 1996;3:21-28.
    • (1996) Chem. Biol. , vol.3 , pp. 21-28
    • Walsh, C.1    Fisher, S.L.2    Park, I.S.3    Prahald, M.4    Wu, Z.5
  • 10
    • 0026355435 scopus 로고
    • Molecular basis for vancomycin resistance in Enterococcus faecium BM 4147: Biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA
    • Bugg TD, Wright GD, Dutka-Malen S, Arthur M, Courvalin P, Walsh C. Molecular basis for vancomycin resistance in Enterococcus faecium BM 4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA. Biochemistry 1991;30: 10408-10415.
    • (1991) Biochemistry , vol.30 , pp. 10408-10415
    • Bugg, T.D.1    Wright, G.D.2    Dutka-Malen, S.3    Arthur, M.4    Courvalin, P.5    Walsh, C.6
  • 11
    • 0035118597 scopus 로고    scopus 로고
    • Restoration of vancomycin susceptibility in Enterococcus faecalis by antiresistance determinant gene transfer
    • Torres Viera C, Tsiodras S, Gold HS, et al. Restoration of vancomycin susceptibility in Enterococcus faecalis by antiresistance determinant gene transfer. Antimicrob Agents Chemother 2001;45:973-975.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 973-975
    • Torres Viera, C.1    Tsiodras, S.2    Gold, H.S.3
  • 12
    • 0026658877 scopus 로고
    • The VanS-VanR two component regulatory system controls synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147
    • Arthur M, Molinas C, Courvalin P. The VanS-VanR two component regulatory system controls synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147. J Bacteriol 1992;174:2582-2591.
    • (1992) J. Bacteriol. , vol.174 , pp. 2582-2591
    • Arthur, M.1    Molinas, C.2    Courvalin, P.3
  • 13
    • 0032870104 scopus 로고    scopus 로고
    • Regulated interactions between partner and non-partner sensors and response regulators that control glycopeptide resistance gene expression in enterococci
    • Arthur M, Depardieu F, Courvalin P. Regulated interactions between partner and non-partner sensors and response regulators that control glycopeptide resistance gene expression in enterococci. Microbiology 1999;145: 1849-1858.
    • (1999) Microbiology , vol.145 , pp. 1849-1858
    • Arthur, M.1    Depardieu, F.2    Courvalin, P.3
  • 14
    • 0028204226 scopus 로고
    • Identification of the DNA-binding site for the phosphorylated VanR protein required for vancomycin resistance in Enterococcus faecium
    • Holman T, Wu Z, Wanner B, Walsh C. Identification of the DNA-binding site for the phosphorylated VanR protein required for vancomycin resistance in Enterococcus faecium. Biochemistry 1994;33:4625-4631.
    • (1994) Biochemistry , vol.33 , pp. 4625-4631
    • Holman, T.1    Wu, Z.2    Wanner, B.3    Walsh, C.4
  • 15
    • 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, Depardieu F, Gerbaud G, Galimand M, Leclercq R, Courvalin P. 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 1997;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
  • 17
    • 0031566835 scopus 로고    scopus 로고
    • Dissemination in Japanese hospitals of strains of Staphylococcus aureus heterogeneously resistant to vancomycin
    • Hiramatsu K, Aritaka N, Hanaki H, et al. Dissemination in Japanese hospitals of strains of Staphylococcus aureus heterogeneously resistant to vancomycin. Lancet 1997; 350:1670-1673.
    • (1997) Lancet , vol.350 , pp. 1670-1673
    • Hiramatsu, K.1    Aritaka, N.2    Hanaki, H.3
  • 18
    • 0005940697 scopus 로고    scopus 로고
    • Combination genetic pharmacological therapy for the treatment of drug resistant and susceptible HIV-1
    • Inouye R, Gillis J, Hammer SM. Combination genetic pharmacological therapy for the treatment of drug resistant and susceptible HIV-1. Antivir Ther 1999;4(Suppl 1):121.
    • (1999) Antivir. Ther. , vol.4 , Issue.SUPPL. 1 , pp. 121
    • Inouye, R.1    Gillis, J.2    Hammer, S.M.3
  • 19
    • 0032922742 scopus 로고    scopus 로고
    • Antisense RNA. Gene therapy for studying and modulating biological processes
    • Weiss B, Davidkova G, Zhou LW, Antisense RNA. gene therapy for studying and modulating biological processes. Cell Mol Life Sci 1999;55:334-358.
    • (1999) Cell Mol. Life Sci. , vol.55 , pp. 334-358
    • Weiss, B.1    Davidkova, G.2    Zhou, L.W.3
  • 21
    • 0029262020 scopus 로고
    • Antisense approaches to cancer gene therapy
    • Mercola D, Cohen JS. Antisense approaches to cancer gene therapy. Cancer Gene Ther 1995;2:47-59.
    • (1995) Cancer Gene Ther. , vol.2 , pp. 47-59
    • Mercola, D.1    Cohen, J.S.2
  • 22
    • 0024561489 scopus 로고
    • Enzymes in the D-alanine branch of bacterial cell wall peptidoglycan assembly
    • Walch C. Enzymes in the D-alanine branch of bacterial cell wall peptidoglycan assembly. J Biol Chem 1989;264: 2392-2396.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2392-2396
    • Walch, C.1
  • 23
    • 0029996927 scopus 로고    scopus 로고
    • Evolution of structure and substrate specificity in D-alanine:D-alanine ligases and related enzymes
    • Evers S, Casadewall B, Charles M, Dutka-Malen S, Galimand M, Courvalin P. Evolution of structure and substrate specificity in D-alanine:D-alanine ligases and related enzymes. J Mol Evol 1996;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
  • 24
    • 0024355483 scopus 로고
    • Structure, biochemistry and mechanism of action of glycopeptide antibiotics
    • Reynolds PE. Structure, biochemistry and mechanism of action of glycopeptide antibiotics. Eur J Clin Microbiol Infect Dis 1989;8:943-950.
    • (1989) Eur. J. Clin. Microbiol. Infect. Dis. , vol.8 , pp. 943-950
    • Reynolds, P.E.1
  • 25
    • 0028209926 scopus 로고
    • Sequence of the vanB and ddl genes encoding D-alanine: D-lactate and D-alanine:D-alanine ligases in vancomycin resistant Enterococcus faecalis V583
    • Evers S, Reynolds PE, Courvalin P. Sequence of the vanB and ddl genes encoding D-alanine: D-lactate and D-alanine:D-alanine ligases in vancomycin resistant Enterococcus faecalis V583. Gene 1994;140:87-102.
    • (1994) Gene , vol.140 , pp. 87-102
    • Evers, S.1    Reynolds, P.E.2    Courvalin, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.