메뉴 건너뛰기




Volumn 42, Issue 7, 1998, Pages 1542-1548

Selection and characterization of β-lactam-β-lactamase inactivator- resistant mutants following PCR mutagenesis of the TEM-1 β-lactamase gene

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN PLUS CLAVULANIC ACID; AZTREONAM; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; BETA LACTAMASE TEM 1; CEFALORIDINE; CEFALOTIN; CEFEPIME; CEFTAZIDIME; CEFTRIAXONE; KANAMYCIN; SULBACTAM; TAZOBACTAM; UNCLASSIFIED DRUG;

EID: 0031834415     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.42.7.1542     Document Type: Article
Times cited : (63)

References (31)
  • 2
  • 3
    • 0027370236 scopus 로고
    • Characterization of a new TEM-type β-lactamase resistant to clavulanate, sulbactam, and tazobactam in a clinical isolate of Escherichia coli
    • Blasquez, J., M.-R. Baquero, R. Canton, I. Alos, and F. Baquero. 1993. Characterization of a new TEM-type β-lactamase resistant to clavulanate, sulbactam, and tazobactam in a clinical isolate of Escherichia coli. Antimicrob. Agents Chemother. 37:2059-2063.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 2059-2063
    • Blasquez, J.1    Baquero, M.-R.2    Canton, R.3    Alos, I.4    Baquero, F.5
  • 4
    • 0028954421 scopus 로고
    • Complementary roles of mutations at positions 69 and 242 in a class a β-lactamase
    • Bonomo, R. A., C. G. Dawes, J. R. Knox, and D. M. Shlaes. 1995. Complementary roles of mutations at positions 69 and 242 in a class A β-lactamase. Biochim. Biophys. Acta 1247:113-120.
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 113-120
    • Bonomo, R.A.1    Dawes, C.G.2    Knox, J.R.3    Shlaes, D.M.4
  • 5
    • 0029764094 scopus 로고    scopus 로고
    • Characterization of an inhibitor-resistant enzyme IRT-2 derived from TEM-2 β-lactamase produced by Proteus mirabilis strains
    • Bret, L., C. Chanal, D. Sirot, R. Labia, and J. Sirot. 1996. Characterization of an inhibitor-resistant enzyme IRT-2 derived from TEM-2 β-lactamase produced by Proteus mirabilis strains. J. Antimicrob. Chemother. 38:183-191.
    • (1996) J. Antimicrob. Chemother. , vol.38 , pp. 183-191
    • Bret, L.1    Chanal, C.2    Sirot, D.3    Labia, R.4    Sirot, J.5
  • 6
    • 0029842442 scopus 로고    scopus 로고
    • Inhibition of TEM-2 β-lactamase from Escherichia coli by clavulanic acid: Observation of intermediates by electrospray ionization mass spectrometry
    • Brown, R. P., R. T. Aplin, and C. J. Schofield. 1996. Inhibition of TEM-2 β-lactamase from Escherichia coli by clavulanic acid: observation of intermediates by electrospray ionization mass spectrometry. Biochemistry 35:12421-12432.
    • (1996) Biochemistry , vol.35 , pp. 12421-12432
    • Brown, R.P.1    Aplin, R.T.2    Schofield, C.J.3
  • 7
    • 0028246175 scopus 로고
    • Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to β-lactamase inhibitors
    • Brun, T., J. Peduzzi, M. M. Canica, G. Paul, P. Nevot, M. Barthelemy, and R. Labia. 1994. Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to β-lactamase inhibitors. FEMS Microbiol. Lett. 120:111-118.
    • (1994) FEMS Microbiol. Lett. , vol.120 , pp. 111-118
    • Brun, T.1    Peduzzi, J.2    Canica, M.M.3    Paul, G.4    Nevot, P.5    Barthelemy, M.6    Labia, R.7
  • 9
    • 0027515959 scopus 로고
    • Kinetic interactions of tazobactam with β-lactamases from all major structural classes
    • Bush, K., C. Macalintal, B. A. Rasmussen, V. J. Lee, and Y. Yang. 1993. Kinetic interactions of tazobactam with β-lactamases from all major structural classes. Antimicrob. Agents Chemother. 37:851-858.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 851-858
    • Bush, K.1    Macalintal, C.2    Rasmussen, B.A.3    Lee, V.J.4    Yang, Y.5
  • 11
    • 0028798040 scopus 로고
    • Molecular characterization of nine different types of mutants among 107 inhibitor-resistant TEM β-lactamases from clinical isolates of Escherichia coli
    • Henquell, C., C. Chanal, D. Sirot, R. Labia, and J. Sirot. 1995. Molecular characterization of nine different types of mutants among 107 inhibitor-resistant TEM β-lactamases from clinical isolates of Escherichia coli. Antimicrob. Agents Chemother. 39:427-430.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 427-430
    • Henquell, C.1    Chanal, C.2    Sirot, D.3    Labia, R.4    Sirot, J.5
  • 12
    • 0028357710 scopus 로고
    • A structurebased analysis of the inhibition of class A β-lactamases by sulbactam
    • Imtiaz, U., E. M. Billings, J. R. Knox, and S. Mobashery. 1994. A structurebased analysis of the inhibition of class A β-lactamases by sulbactam. Biochemistry 33:5728-5738.
    • (1994) Biochemistry , vol.33 , pp. 5728-5738
    • Imtiaz, U.1    Billings, E.M.2    Knox, J.R.3    Mobashery, S.4
  • 13
    • 0027316253 scopus 로고
    • Inactivation of class a β-lactamases by clavulanic acid: The role of arginine-244 in a non-concerted sequence of events
    • Imtiaz, U., E. M. Billings, J. R. Knox, E. K. Manavathu, S. A. Lerner, and S. Mobashery. 1993. Inactivation of class A β-lactamases by clavulanic acid: the role of arginine-244 in a non-concerted sequence of events. J. Am. Chem. Soc. 115:4435-4442.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4435-4442
    • Imtiaz, U.1    Billings, E.M.2    Knox, J.R.3    Manavathu, E.K.4    Lerner, S.A.5    Mobashery, S.6
  • 14
    • 0025092290 scopus 로고
    • Role of the conserved amino acids of the SDN loop (Ser-130, Asp-131, and Asn-132) in a class a β-lactamase studied by site-directed mutagenesis
    • Jacob, F., B. Joris, S. Lepage, J. Dusart, and J.-M. Frère. 1990. Role of the conserved amino acids of the SDN loop (Ser-130, Asp-131, and Asn-132) in a class A β-lactamase studied by site-directed mutagenesis. Biochem. J. 271:399-406.
    • (1990) Biochem. J. , vol.271 , pp. 399-406
    • Jacob, F.1    Joris, B.2    Lepage, S.3    Dusart, J.4    Frère, J.-M.5
  • 15
    • 0027275788 scopus 로고
    • Crystal structure of Escherichia coli TEM1 β-lactamase at 1.8 Å resolution
    • Jelsch, C., L. Mourey, J. M. Mason, and J.-P. Samama. 1993. Crystal structure of Escherichia coli TEM1 β-lactamase at 1.8 Å resolution. Proteins 16: 364-383.
    • (1993) Proteins , vol.16 , pp. 364-383
    • Jelsch, C.1    Mourey, L.2    Mason, J.M.3    Samama, J.-P.4
  • 16
    • 0028821830 scopus 로고
    • Extended-spectrum and inhibitor-resistant TEM-type β-lactamases: Mutations, specificity, and three-dimensional structure
    • Knox, J. R. 1995. Extended-spectrum and inhibitor-resistant TEM-type β-lactamases: mutations, specificity, and three-dimensional structure. Antimicrob. Agents Chemother. 39:2593-2601.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2593-2601
    • Knox, J.R.1
  • 17
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 18
    • 0026504625 scopus 로고
    • Streptomyces albus G serine β-lactamase. Probing of the catalytic mechanism via molecular modeling of mutant enzymes
    • Lamotte-Brasseur, J., F. Jacob-Dubuisson, G. Dive, J.-M. Frère, and J.-M. Ghuysen. 1992. Streptomyces albus G serine β-lactamase. Probing of the catalytic mechanism via molecular modeling of mutant enzymes. Biochem. J. 282:189-195.
    • (1992) Biochem. J. , vol.282 , pp. 189-195
    • Lamotte-Brasseur, J.1    Jacob-Dubuisson, F.2    Dive, G.3    Frère, J.-M.4    Ghuysen, J.-M.5
  • 19
    • 0028823277 scopus 로고
    • First characterization of inhibitor-resistant TEM (IRT) β-lactamases in Klebsiella pneumoniae strains
    • Lemozy, J., D. Sirot, C. Chanal, C. Hue, R. Labia, H. Dabernat, and J. Sirot. 1995. First characterization of inhibitor-resistant TEM (IRT) β-lactamases in Klebsiella pneumoniae strains. Antimicrob. Agents Chemother. 33:2580-2582.
    • (1995) Antimicrob. Agents Chemother. , vol.33 , pp. 2580-2582
    • Lemozy, J.1    Sirot, D.2    Chanal, C.3    Hue, C.4    Labia, R.5    Dabernat, H.6    Sirot, J.7
  • 21
    • 0028802117 scopus 로고
    • Contribution of mutant analysis to the understanding of enzyme catalysis: The case of class A β-lactamases
    • Matagne, A., and J.-M. Frère. 1995. Contribution of mutant analysis to the understanding of enzyme catalysis: the case of class A β-lactamases. Biochim. Biophys. Acta 1246:109-126.
    • (1995) Biochim. Biophys. Acta , vol.1246 , pp. 109-126
    • Matagne, A.1    Frère, J.-M.2
  • 22
    • 0024358138 scopus 로고
    • An efficient method for generating proteins with altered enzymatic properties: Application to β-lactamase
    • Oliphant, A. R., and K. Struhl. 1989. An efficient method for generating proteins with altered enzymatic properties: application to β-lactamase. Proc. Natl. Acad. Sci. USA 86:9094-9098.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9094-9098
    • Oliphant, A.R.1    Struhl, K.2
  • 24
    • 0025869458 scopus 로고
    • Factors determining resistance to β-lactam combined with β-lactamase inhibitors in Escherichia coli
    • Reguera, J. A., F. Baquero, J. C. Penez-Diaz, and J. L. Martinez. 1991. Factors determining resistance to β-lactam combined with β-lactamase inhibitors in Escherichia coli. J. Antimicrob. Chemother. 27:569-575.
    • (1991) J. Antimicrob. Chemother. , vol.27 , pp. 569-575
    • Reguera, J.A.1    Baquero, F.2    Penez-Diaz, J.C.3    Martinez, J.L.4
  • 25
    • 0023688186 scopus 로고
    • Resistance to ticarcillin-potassium clavulanate among clinical isolates of the family Enterobacteriaceae: Role of PSE-1 β-lactamase and high levels of TEM-1 and SHV-1 and problems with false susceptibility in disk diffusion tests
    • Sanders, C. C., J. P. Iaconis, G. P. Bodey, and G. Samonis. 1988. Resistance to ticarcillin-potassium clavulanate among clinical isolates of the family Enterobacteriaceae: role of PSE-1 β-lactamase and high levels of TEM-1 and SHV-1 and problems with false susceptibility in disk diffusion tests. Antimicrob. Agents Chemother. 32:1365-1369.
    • (1988) Antimicrob. Agents Chemother. , vol.32 , pp. 1365-1369
    • Sanders, C.C.1    Iaconis, J.P.2    Bodey, G.P.3    Samonis, G.4
  • 26
    • 0029120340 scopus 로고
    • The asparagine to aspartic acid substitution at position 276 of TEM-35 and TEM-36 is involved in the β-lactamase resistance to clavulanic acid
    • Saves, I., O. Burlet-Schiltz, P. Swaren, F. Lefevre, J.-M. Masson, J.-C. Prome, and J.-P. Samama. 1995. The asparagine to aspartic acid substitution at position 276 of TEM-35 and TEM-36 is involved in the β-lactamase resistance to clavulanic acid. J. Biol. Chem. 270:18240-18245.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18240-18245
    • Saves, I.1    Burlet-Schiltz, O.2    Swaren, P.3    Lefevre, F.4    Masson, J.-M.5    Prome, J.-C.6    Samama, J.-P.7
  • 27
    • 0028894848 scopus 로고
    • Incidence and mechanisms of resistance to the combination of amoxicillin and clavulanic acid in Escherichia coli
    • Stapleton, P., P.-J. Wu, A. King, K. Shannon, G. French, and I. Phillips. 1995. Incidence and mechanisms of resistance to the combination of amoxicillin and clavulanic acid in Escherichia coli. Antimicrob. Agents Chemother. 39:2478-2483.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2478-2483
    • Stapleton, P.1    Wu, P.-J.2    King, A.3    Shannon, K.4    French, G.5    Phillips, I.6
  • 28
    • 0027238119 scopus 로고
    • Selection of variants of the TEM-1 β-lactamase, encoded by a plasmid of clinical origin, with increased resistance to β-lactamase inhibitors
    • Thomson, C. J., and S. G. B. Amyes. 1993. Selection of variants of the TEM-1 β-lactamase, encoded by a plasmid of clinical origin, with increased resistance to β-lactamase inhibitors. J. Antimicrob. Chemother. 31:655-664.
    • (1993) J. Antimicrob. Chemother. , vol.31 , pp. 655-664
    • Thomson, C.J.1    Amyes, S.G.B.2
  • 29
    • 0026437823 scopus 로고
    • Clinical isolates of Escherichia coli producing TRI β-lactamases: Novel TEM-enzymes conferring resistance to β-lactamase inhibitors
    • Vedel, G., A. Belaaouaj, L. Gilly, A. Philippon, P. Nevot, and G. Paul. 1992. Clinical isolates of Escherichia coli producing TRI β-lactamases: novel TEM-enzymes conferring resistance to β-lactamase inhibitors. J. Antimicrob. Chemother. 30:449-462.
    • (1992) J. Antimicrob. Chemother. , vol.30 , pp. 449-462
    • Vedel, G.1    Belaaouaj, A.2    Gilly, L.3    Philippon, A.4    Nevot, P.5    Paul, G.6
  • 30
    • 0026654218 scopus 로고
    • Elucidation of the role of arginine-244 in the turnover process of class A β-lactamases
    • Zafaralla, G., E. K. Manavathu, S. A. Lerner, and S. Mobashery. 1992. Elucidation of the role of arginine-244 in the turnover process of class A β-lactamases. Biochemistry 31:3847-3852.
    • (1992) Biochemistry , vol.31 , pp. 3847-3852
    • Zafaralla, G.1    Manavathu, E.K.2    Lerner, S.A.3    Mobashery, S.4
  • 31
    • 0028302091 scopus 로고
    • Emergence of clinical isolates of Escherichia coli producing TEM-1 derivatives or an OXA-1 β-lactamase conferring resistance to β-lactamase inhibitors
    • Zhou, X. Y., F. Bordon, D. Sirot, M.-D. Kitzis, and L. Gutmann. 1994. Emergence of clinical isolates of Escherichia coli producing TEM-1 derivatives or an OXA-1 β-lactamase conferring resistance to β-lactamase inhibitors. Antimicrob. Agents Chemother. 38:1085-1089.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1085-1089
    • Zhou, X.Y.1    Bordon, F.2    Sirot, D.3    Kitzis, M.-D.4    Gutmann, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.