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Volumn 179, Issue 21, 1997, Pages 6756-6763

Cloning of the Staphylococcus aureus ddh gene encoding NAD+-dependent D-lactate dehydrogenase and insertional inactivation in a glycopeptide- resistant isolate

Author keywords

[No Author keywords available]

Indexed keywords

DEXTRO LACTATE DEHYDROGENASE; GLYCOPEPTIDE; VANCOMYCIN;

EID: 0030696219     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.21.6756-6763.1997     Document Type: Article
Times cited : (26)

References (45)
  • 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. 174:2583-2591.
    • (1992) J. Bacteriol. , vol.174 , pp. 2583-2591
    • Arthur, M.1    Molinas, C.2    Courvalin, P.3
  • 2
    • 0025741584 scopus 로고
    • Structural relationship between the vancomycin resistance protein VanH and 2-hydroxycarboxylic acid
    • Arthur, M., C. Molinas, S. Dutka-Malen, and P. Courvalin. 1991. Structural relationship between the vancomycin resistance protein VanH and 2-hydroxycarboxylic acid. Gene 103:133-134.
    • (1991) Gene , vol.103 , pp. 133-134
    • Arthur, M.1    Molinas, C.2    Dutka-Malen, S.3    Courvalin, P.4
  • 4
    • 0025079412 scopus 로고
    • Transformation of Staphylococcus epidermidis and other staphylococcal species with plasmid DNA by electroporation
    • Augustin, J., and F. Götz. 1990. Transformation of Staphylococcus epidermidis and other staphylococcal species with plasmid DNA by electroporation. FEMS Microbiol. Lett. 66:203-208.
    • (1990) FEMS Microbiol. Lett. , vol.66 , pp. 203-208
    • Augustin, J.1    Götz, F.2
  • 6
    • 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
  • 7
    • 0026057838 scopus 로고
    • Development of in-vitro resistance to glycopeptide antibiotics: Assessment in staphylococci of different species
    • Biavasco, F., E. Giovanetti, M. P. Montanari, R. Lupidi, and P. E. Varaldo. 1991. Development of in-vitro resistance to glycopeptide antibiotics: assessment in staphylococci of different species. J. Antimicrob. Chemother. 27:71-79.
    • (1991) J. Antimicrob. Chemother. , vol.27 , pp. 71-79
    • Biavasco, F.1    Giovanetti, E.2    Montanari, M.P.3    Lupidi, R.4    Varaldo, P.E.5
  • 8
    • 0029750226 scopus 로고    scopus 로고
    • Peptidoglycan synthesis and structure in Staphylococcus haemolyticus expressing increasing levels of resistance to glycopeptide antibiotics
    • Billot-Klein, D., L. Gutmann, D. Bryant, D. Bell, J. van Heijenoort, J. Grewal, and D. M. Shlaes. 1996. Peptidoglycan synthesis and structure in Staphylococcus haemolyticus expressing increasing levels of resistance to glycopeptide antibiotics. J. Bacteriol. 178:4696-4703.
    • (1996) J. Bacteriol. , vol.178 , pp. 4696-4703
    • Billot-Klein, D.1    Gutmann, L.2    Bryant, D.3    Bell, D.4    Van Heijenoort, J.5    Grewal, J.6    Shlaes, D.M.7
  • 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
    • 0026073599 scopus 로고
    • Identification of vancomycin resistance protein Vana as a D-alanine: D-alanine ligase of altered substrate specificity
    • Bugg, 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, D.H.1    Dutka-Malen, S.2    Arthur, M.3    Courvalin, P.4    Walsh, C.T.5
  • 11
    • 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., 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.1    Wright, G.D.2    Dutka-Malen, S.3    Arthur, M.4    Courvalin, P.5    Walsh, C.T.6
  • 13
    • 85036486027 scopus 로고    scopus 로고
    • Personal communication
    • 12a.Clark, D. P. Personal communication.
    • Clark, D.P.1
  • 14
    • 0026756474 scopus 로고
    • Characterization of Staphylococcus aureus isolates with decreased susceptibility to vancomycin and teicoplanin: Isolation and purification of a constitutively produced protein associated with decreased susceptibility
    • Daum, R. S., S. Gupta, R. Sabbagh, and W. M. Milewski. 1992. Characterization of Staphylococcus aureus isolates with decreased susceptibility to vancomycin and teicoplanin: isolation and purification of a constitutively produced protein associated with decreased susceptibility. J. Infect. Dis. 166:1066-1072.
    • (1992) J. Infect. Dis. , vol.166 , pp. 1066-1072
    • Daum, R.S.1    Gupta, S.2    Sabbagh, R.3    Milewski, W.M.4
  • 15
    • 0027518660 scopus 로고
    • The vanB gene of vancomycin resistant Enterococcus faecalis V583 is structurally related to 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 D-Ala-D-Ala ligases and glycopeptide resistance proteins vanA and vanC. Gene 24:143-144.
    • (1993) Gene , vol.24 , pp. 143-144
    • Evers, S.1    Sahm, D.F.2    Courvalin, P.3
  • 16
    • 0024485336 scopus 로고
    • Mutants of Escherichia coli deficient in fermentative lactate dehydrogenase
    • Fairoz, M.-J., Y. A. Kiswar, and D. P. Clark. 1989. Mutants of Escherichia coli deficient in fermentative lactate dehydrogenase. J. Bacteriol. 171:342-348.
    • (1989) J. Bacteriol. , vol.171 , pp. 342-348
    • Fairoz, M.-J.1    Kiswar, Y.A.2    Clark, D.P.3
  • 17
    • 0021381028 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Addendum
    • Feinberg, A. P., and B. Vogelstein. 1984. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 137:266-267. (Addendum.)
    • (1984) Anal. Biochem. , vol.137 , pp. 266-267
    • Feinberg, A.P.1    Vogelstein, B.2
  • 18
    • 0014233764 scopus 로고
    • Regulation of Staphylococcus aureus lactate dehydrogenase
    • Garrard, W., and J. Lascelles. 1968. Regulation of Staphylococcus aureus lactate dehydrogenase. J. Bacteriol. 95:152-156.
    • (1968) J. Bacteriol. , vol.95 , pp. 152-156
    • Garrard, W.1    Lascelles, J.2
  • 19
    • 0018818947 scopus 로고
    • Bacterial lactate dehydrogenases
    • Garvie, E. I. 1980. Bacterial lactate dehydrogenases. Microbiol. Rev. 44:106-139.
    • (1980) Microbiol. Rev. , vol.44 , pp. 106-139
    • Garvie, E.I.1
  • 20
    • 0017075242 scopus 로고
    • Comparative biochemistry of lactate dehydrogenases from staphylococci, p. 245-252
    • J. Jeljaszewicz (ed.), Gustav Fisher Verlag, Stuttgart, Germany
    • Götz, F., and K. H. Schleifer. 1976. Comparative biochemistry of lactate dehydrogenases from staphylococci, p. 245-252. In J. Jeljaszewicz (ed.), Staphylococci and staphylococcal diseases. Gustav Fisher Verlag, Stuttgart, Germany.
    • (1976) Staphylococci and Staphylococcal Diseases
    • Götz, F.1    Schleifer, K.H.2
  • 21
    • 0023202922 scopus 로고
    • A comparison of the responses of staphylococci and streptococci to teicoplanin and vancomycin
    • Greenwood, D., K. Bidgood, and M. Turner. 1987. A comparison of the responses of staphylococci and streptococci to teicoplanin and vancomycin. J. Antimicrob. Chemother. 20:155-164.
    • (1987) J. Antimicrob. Chemother. , vol.20 , pp. 155-164
    • Greenwood, D.1    Bidgood, K.2    Turner, M.3
  • 22
    • 0028256317 scopus 로고
    • Alterations in peptidoglycan precursors and vancomycin susceptibility in Tn917 insertion mutants of Enterococcus faecalis 221
    • Handwerger, S. 1994. Alterations in peptidoglycan precursors and vancomycin susceptibility in Tn917 insertion mutants of Enterococcus faecalis 221. Antimicrob. Agents Chemother. 38:473-475.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 473-475
    • Handwerger, S.1
  • 23
    • 0027972697 scopus 로고
    • Vancomycin-resistant Leuconostoc mesenteroides and Lactobacillus casei synthesize cytoplasmic precursors that terminate in lactate
    • Handwerger, S., M. J. Pucci, K. J. Volk, J. Liu, and M. S. Lee. 1994. Vancomycin-resistant Leuconostoc mesenteroides and Lactobacillus casei synthesize cytoplasmic precursors that terminate in lactate. J. Bacteriol. 176: 260-264.
    • (1994) J. Bacteriol. , vol.176 , pp. 260-264
    • Handwerger, S.1    Pucci, M.J.2    Volk, K.J.3    Liu, J.4    Lee, M.S.5
  • 24
    • 0026337049 scopus 로고
    • In vitro selection of resistance to vancomycin in bloodstream isolates of Staphylococcus haemolyticus and Staphylococcus epidermidis
    • Herwaldt, L., L. Boykin, and M. Pfaller. 1991. In vitro selection of resistance to vancomycin in bloodstream isolates of Staphylococcus haemolyticus and Staphylococcus epidermidis. Eur. J. Clin. Microbiol. Infect. Dis. 10:1007-1012.
    • (1991) Eur. J. Clin. Microbiol. Infect. Dis. , vol.10 , pp. 1007-1012
    • Herwaldt, L.1    Boykin, L.2    Pfaller, M.3
  • 26
    • 0025372366 scopus 로고
    • Emergence of teicoplanin resistance during therapy of Staphylococcus aureus endocarditis
    • Kaatz, G. W., S. M. Seo, N. J. Dorman, and S. A. Lerner. 1990. Emergence of teicoplanin resistance during therapy of Staphylococcus aureus endocarditis. J. Infect. Dis. 162:103-108.
    • (1990) J. Infect. Dis. , vol.162 , pp. 103-108
    • Kaatz, G.W.1    Seo, S.M.2    Dorman, N.J.3    Lerner, S.A.4
  • 28
    • 0030246884 scopus 로고    scopus 로고
    • A highly vancomycin resistant laboratory mutant of Staphylococcus aureus
    • Krzysztof, S., and A. Tomasz. 1996. A highly vancomycin resistant laboratory mutant of Staphylococcus aureus. FEMS Microbiol. Lett. 142:161-166.
    • (1996) FEMS Microbiol. Lett. , vol.142 , pp. 161-166
    • Krzysztof, S.1    Tomasz, A.2
  • 29
    • 0024437119 scopus 로고
    • Construction, transfer and properties of a novel temperature-sensitive integrable plasmid for genomic analysis of Staphylococcus aureus
    • Luchansky, J. B., A. K. Benson, and A. G. Atherly. 1989. Construction, transfer and properties of a novel temperature-sensitive integrable plasmid for genomic analysis of Staphylococcus aureus. Mol. Microbiol. 3:65-78.
    • (1989) Mol. Microbiol. , vol.3 , pp. 65-78
    • Luchansky, J.B.1    Benson, A.K.2    Atherly, A.G.3
  • 30
    • 0028999211 scopus 로고
    • Decreased teicoplanin susceptibility of methicillin resistant strains of Staphylococcus aureus
    • Mainardi, J. L., D. M. Shlaes, R. V. Goering, J. Shlaes, J. F. Acar, and F. W. Goldstein. 1995. Decreased teicoplanin susceptibility of methicillin resistant strains of Staphylococcus aureus. J. Infect. Dis. 171:1646-1650.
    • (1995) J. Infect. Dis. , vol.171 , pp. 1646-1650
    • Mainardi, J.L.1    Shlaes, D.M.2    Goering, R.V.3    Shlaes, J.4    Acar, J.F.5    Goldstein, F.W.6
  • 32
    • 0030872458 scopus 로고    scopus 로고
    • Increased production of penicillin-binding protein 2, increased detection of other penicillin-binding proteins, and decreased coagulase activity associated with glycopeptide resistance in Staphylococcus aureus
    • Moreira, B., S. Boyle-Vavra, B. L. M. de Jonge, and R. S. Daum. 1997. Increased production of penicillin-binding protein 2, increased detection of other penicillin-binding proteins, and decreased coagulase activity associated with glycopeptide resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 41:1788-1793.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1788-1793
    • Moreira, B.1    Boyle-Vavra, S.2    De Jonge, B.L.M.3    Daum, R.S.4
  • 33
    • 0027475377 scopus 로고
    • Isolation and characterization of transposon mutants of Staphylococcus epidermidis deficient in capsular polysaccharide/adhesin and slime
    • Muller, E., J. Hübner, N. Gutierrez, S. Takeda, D. A. Goldmann, and G. B. Pier. 1993. Isolation and characterization of transposon mutants of Staphylococcus epidermidis deficient in capsular polysaccharide/adhesin and slime. Infect. Immun. 61:551-558.
    • (1993) Infect. Immun. , vol.61 , pp. 551-558
    • Muller, E.1    Hübner, J.2    Gutierrez, N.3    Takeda, S.4    Goldmann, D.A.5    Pier, G.B.6
  • 35
    • 0025837196 scopus 로고
    • Genetic systems in staphylococci
    • Novick, R. N. 1991. Genetic systems in staphylococci. Methods Enzymol. 204:587-636.
    • (1991) Methods Enzymol. , vol.204 , pp. 587-636
    • Novick, R.N.1
  • 36
    • 0027070370 scopus 로고
    • Novel membrane proteins present in teicoplanin-resistant, vancomycin sensitive, coagulase-negative staphylococcus spp
    • O'Hare, M. D., and P. Reynolds. 1992. Novel membrane proteins present in teicoplanin-resistant, vancomycin sensitive, coagulase-negative staphylococcus spp. J. Antimicrob. Chemother. 30:753-768.
    • (1992) J. Antimicrob. Chemother. , vol.30 , pp. 753-768
    • O'Hare, M.D.1    Reynolds, P.2
  • 37
    • 0029845799 scopus 로고    scopus 로고
    • Gain of D-alanyl-D-lactate or D-lactyl-D-alanine synthetase activities in three active-site mutants of the Escherichia coli D-alanyl-D-alanine ligase B
    • Park, I., C. Lin, and C. Walsh. 1996. Gain of D-alanyl-D-lactate or D-lactyl-D-alanine synthetase activities in three active-site mutants of the Escherichia coli D-alanyl-D-alanine ligase B. Biochemistry 35:10464-10471.
    • (1996) Biochemistry , vol.35 , pp. 10464-10471
    • Park, I.1    Lin, C.2    Walsh, C.3
  • 39
    • 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
  • 41
    • 0027483966 scopus 로고
    • Teicoplanin-resistant Staphylococcus aureus expresses a novel membrane protein and increases expression of penicillin-binding protein 2 complex
    • Shlaes, D. M., J. H. Shlaes, S. Vincent, L. Etter, P. D. Fey, and R. V. Goering. 1993. Teicoplanin-resistant Staphylococcus aureus expresses a novel membrane protein and increases expression of penicillin-binding protein 2 complex. Antimicrob. Agents Chemother. 37:2432-2437.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 2432-2437
    • Shlaes, D.M.1    Shlaes, J.H.2    Vincent, S.3    Etter, L.4    Fey, P.D.5    Goering, R.V.6
  • 42
    • 0014429554 scopus 로고
    • Chemical characterization of D-lactate dehydrogenase from Escherichia coli B
    • Tarmy, E. M., and N. O. Kaplan. 1959. Chemical characterization of D-lactate dehydrogenase from Escherichia coli B. J. Biol. Chem. 243:2579-2586.
    • (1959) J. Biol. Chem. , vol.243 , pp. 2579-2586
    • Tarmy, E.M.1    Kaplan, N.O.2
  • 43
    • 0014429571 scopus 로고
    • Kinetics of Escherichia coli B D-lactate dehydrogenase and evidence for pyruvate controlled change in conformation
    • Tarmy, E. M., and N. O. Kaplan. 1968. Kinetics of Escherichia coli B D-lactate dehydrogenase and evidence for pyruvate controlled change in conformation. J. Biol. Chem. 243:2587-2596.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2587-2596
    • Tarmy, E.M.1    Kaplan, N.O.2
  • 44
    • 0002522539 scopus 로고
    • Plasmid vectors for recovering and exploiting Tn917 transpositions in Bacillus and other Gram-positive bacteria
    • K. G. Hardy (ed.), IRL Press, Oxford, United Kingdom
    • Youngman, P. 1987. Plasmid vectors for recovering and exploiting Tn917 transpositions in Bacillus and other Gram-positive bacteria, p. 79-103. In K. G. Hardy (ed.), Plasmids: a practical approach. IRL Press, Oxford, United Kingdom.
    • (1987) Plasmids: a Practical Approach , pp. 79-103
    • Youngman, P.1
  • 45
    • 84961012967 scopus 로고
    • Vancomycin, a new antibiotic. II. in vitro antibacterial studies
    • Ziegler, D. W., R. N. Wolfe, and J. M. McGuire. 1955-1956. Vancomycin, a new antibiotic. II. In vitro antibacterial studies. Antibiotics Annu. 1955-1956:612-618.
    • (1955) Antibiotics Annu. , vol.1955-1956 , pp. 612-618
    • Ziegler, D.W.1    Wolfe, R.N.2    McGuire, J.M.3


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