메뉴 건너뛰기




Volumn 48, Issue 8, 2004, Pages 3028-3032

Impact of specific pbp5 mutations on expression of β-lactam resistance in Enterococcus faecium

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMPICILLIN; BETA LACTAM ANTIBIOTIC; METHIONINE; PENICILLIN BINDING PROTEIN; PENICILLIN BINDING PROTEIN 5; PENICILLIN DERIVATIVE; PIPERACILLIN; SERINE; TICARCILLIN; UNCLASSIFIED DRUG;

EID: 3342892900     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.48.8.3028-3032.2004     Document Type: Article
Times cited : (100)

References (16)
  • 1
    • 0031783527 scopus 로고    scopus 로고
    • Genetic linkage and cotransfer of a novel, vanB-containing transposon (Tn5382) and a low-affinity penicillin-binding protein 5 gene in a clinical vancomycin-resistant Enterococcus faecium isolate
    • Carias, L. L., S. D. Rudin, C. J. Donskey, and L. B. Rice. 1998. Genetic linkage and cotransfer of a novel, vanB-containing transposon (Tn5382) and a low-affinity penicillin-binding protein 5 gene in a clinical vancomycin-resistant Enterococcus faecium isolate. J. Bacteriol. 180:4426-4434.
    • (1998) J. Bacteriol. , vol.180 , pp. 4426-4434
    • Carias, L.L.1    Rudin, S.D.2    Donskey, C.J.3    Rice, L.B.4
  • 2
    • 0033558272 scopus 로고    scopus 로고
    • Hydrogen bonding and protein perturbation in beta-lactam acyl-enzymes of Streptococcus pneumoniae penicillin-binding protein PBP2x
    • Chittock, R. S., S. Ward, A. S. Wilkinson, P. Caspers, B. Mensch, M. G. Page, and C. W. Wharton. 1999. Hydrogen bonding and protein perturbation in beta-lactam acyl-enzymes of Streptococcus pneumoniae penicillin-binding protein PBP2x. Biochem. J. 338(Pt 1):153-159.
    • (1999) Biochem. J. , vol.338 , Issue.PART 1 , pp. 153-159
    • Chittock, R.S.1    Ward, S.2    Wilkinson, A.S.3    Caspers, P.4    Mensch, B.5    Page, M.G.6    Wharton, C.W.7
  • 3
    • 0017709445 scopus 로고
    • Beta-turns in proteins
    • Chou, P. Y., and G. D. Fasman. 1977. Beta-turns in proteins. J. Mol. Biol. 115:135-175.
    • (1977) J. Mol. Biol. , vol.115 , pp. 135-175
    • Chou, P.Y.1    Fasman, G.D.2
  • 4
    • 0037701641 scopus 로고    scopus 로고
    • Probing the catalytic activity of a cell division-specific transpeptidase in vivo with beta-lactams
    • Eberhardt, C., L. Kuerschner, and D. S. Weiss. 2003. Probing the catalytic activity of a cell division-specific transpeptidase in vivo with beta-lactams. J. Bacteriol. 185:3726-3734.
    • (2003) J. Bacteriol. , vol.185 , pp. 3726-3734
    • Eberhardt, C.1    Kuerschner, L.2    Weiss, D.S.3
  • 5
    • 0028041404 scopus 로고
    • Overproduction of a low-affinity penicillin-binding protein and high-level ampicillin resistance in Enterococcus faecium
    • Fontana, R., M. Aldegheri, M. Ligozzi, H. Lopez, A. Sucari, and G. Satta. 1994. Overproduction of a low-affinity penicillin-binding protein and high-level ampicillin resistance in Enterococcus faecium. Antimicrob. Agents Chemother. 38:1980-1983.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1980-1983
    • Fontana, R.1    Aldegheri, M.2    Ligozzi, M.3    Lopez, H.4    Sucari, A.5    Satta, G.6
  • 6
    • 0029315603 scopus 로고
    • MAB, a generally applicable molecular force field for structure modelling in medicinal chemistry
    • Gerber, P. R., and K. Muller. 1995. MAB, a generally applicable molecular force field for structure modelling in medicinal chemistry. J. Comput. Aided Mol. Des. 9:251-268.
    • (1995) J. Comput. Aided Mol. Des. , vol.9 , pp. 251-268
    • Gerber, P.R.1    Muller, K.2
  • 7
    • 0034595512 scopus 로고    scopus 로고
    • The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: Implication in drug resistance
    • Gordon, E., N. Mouz, E. Duee, and O. Dideberg. 2000. The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance. J. Mol. Biol. 299:477-485.
    • (2000) J. Mol. Biol. , vol.299 , pp. 477-485
    • Gordon, E.1    Mouz, N.2    Duee, E.3    Dideberg, O.4
  • 8
    • 0022981913 scopus 로고
    • Loops in globular proteins: A novel category of secondary structure
    • Leszczynski, J. F., and G. D. Rose. 1986. Loops in globular proteins: a novel category of secondary structure. Science 234:849-855.
    • (1986) Science , vol.234 , pp. 849-855
    • Leszczynski, J.F.1    Rose, G.D.2
  • 9
    • 0029988098 scopus 로고    scopus 로고
    • X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme
    • Pares, S., N. Mouz, Y. Petillot, R. Hakenbeck, and O. Dideberg. 1996. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat. Struct. Biol. 3:284-289.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 284-289
    • Pares, S.1    Mouz, N.2    Petillot, Y.3    Hakenbeck, R.4    Dideberg, O.5
  • 10
    • 0031573015 scopus 로고    scopus 로고
    • A broad-host-range mobilizable shuttle vector for the construction of transcriptional fusions to beta-galatosidase in gram-positive bacteria
    • Poyart, C., and P. Trieu-Cuot. 1997. A broad-host-range mobilizable shuttle vector for the construction of transcriptional fusions to beta-galatosidase in gram-positive bacteria. FEMS Microbiol. Lett. 156:193-198.
    • (1997) FEMS Microbiol. Lett. , vol.156 , pp. 193-198
    • Poyart, C.1    Trieu-Cuot, P.2
  • 12
    • 0031817529 scopus 로고    scopus 로고
    • Penicillin-binding protein 5 sequence alterations in clinical isolates of Enterococcus faecium with different levels of β-lactam resistance
    • Rybkine, T., J.-L. Mainardi, W. Sougakoff, E. Collatz, and L. Gutmann. 1998. Penicillin-binding protein 5 sequence alterations in clinical isolates of Enterococcus faecium with different levels of β-lactam resistance. J. Infect. Dis. 178:159-163.
    • (1998) J. Infect. Dis. , vol.178 , pp. 159-163
    • Rybkine, T.1    Mainardi, J.-L.2    Sougakoff, W.3    Collatz, E.4    Gutmann, L.5
  • 14
    • 0034863517 scopus 로고    scopus 로고
    • Role of penicillin-binding protein 5 in expression of ampicillin resistance and peptidoglycan structure in Enterococcus faecium
    • Sifaoui, F., M. Arthur, L. Rice, and L. Gutmann. 2001. Role of penicillin-binding protein 5 in expression of ampicillin resistance and peptidoglycan structure in Enterococcus faecium. Antimicrob. Agents Chemother. 45:2594-2597.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 2594-2597
    • Sifaoui, F.1    Arthur, M.2    Rice, L.3    Gutmann, L.4
  • 15
    • 0022393449 scopus 로고
    • One or two low affinity penicillin-binding proteins may be responsible for the range of susceptibility of Enterococcus faecium to penicillin
    • Williamson, R., C. LaBouguenec, L. Gutmann, and T. Horaud. 1985. One or two low affinity penicillin-binding proteins may be responsible for the range of susceptibility of Enterococcus faecium to penicillin. J. Gen. Microbiol. 131:1933-1940.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 1933-1940
    • Williamson, R.1    LaBouguenec, C.2    Gutmann, L.3    Horaud, T.4
  • 16
    • 10144243973 scopus 로고    scopus 로고
    • Structure of the low-affinity penicillin-binding protein 5 PBP5fm in wild-type and highly penicillin-resistant strains of Enterococcus faecium
    • Zorzi, W., X. Y. Zhou, O. Dardenne, J. Lamotte, D. Raze, J. Pierre, L. Gutmann, and J. Coyette. 1996. Structure of the low-affinity penicillin-binding protein 5 PBP5fm in wild-type and highly penicillin-resistant strains of Enterococcus faecium. J. Bacteriol. 178:4948-4957.
    • (1996) J. Bacteriol. , vol.178 , pp. 4948-4957
    • Zorzi, W.1    Zhou, X.Y.2    Dardenne, O.3    Lamotte, J.4    Raze, D.5    Pierre, J.6    Gutmann, L.7    Coyette, J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.