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Volumn 43, Issue 8, 1999, Pages 1881-1887

Construction and characterization of mutants of the TEM-1 β-lactamase containing amino acid substitutions associated with both extended-spectrum resistance and resistance to β-lactamase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

AMOXICILLIN; AZTREONAM; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; CEFALORIDINE; CEFEPIME; CEFOTAXIME; CEFTAZIDIME; CHLORAMPHENICOL; CLAVULANIC ACID; NITROCEFIN; PIPERACILLIN; TAZOBACTAM; TEMOCILLIN; TETRACYCLINE; TICARCILLIN;

EID: 0032816956     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.43.8.1881     Document Type: Article
Times cited : (29)

References (32)
  • 1
  • 2
    • 0030875916 scopus 로고    scopus 로고
    • Construction and characterization of an OHIO-1 β-lactamase bearing Met69Ile and Gly238Ser mutations
    • Bonomo, R. A., J. R. Knox, S. D. Rudin, and D. M. Shlaes. 1997. Construction and characterization of an OHIO-1 β-lactamase bearing Met69Ile and Gly238Ser mutations. Antimicrob. Agents Chemother. 41:1940-1943.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1940-1943
    • Bonomo, R.A.1    Knox, J.R.2    Rudin, S.D.3    Shlaes, D.M.4
  • 4
    • 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. Channel, 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    Channel, C.2    Sirot, D.3    Labia, R.4    Sirot, J.5
  • 5
    • 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. Péduzzi, M. M. Caniça, G. Paul, P. Névot, M. Barthélémy, 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    Péduzzi, J.2    Caniça, M.M.3    Paul, G.4    Névot, P.5    Barthélémy, M.6    Labia, R.7
  • 6
    • 0029071785 scopus 로고
    • A functional classification scheme for β-lactamases and its correlation with molecular structure
    • Bush, K., G. A. Jacoby, and A. A. Medeiros. 1995. A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39:1211-1233.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 8
    • 0030981110 scopus 로고    scopus 로고
    • Are TEM β-lactamases encoded by pBR322 and Bluescript plasmids enzymatically indistinguishable?
    • Chaibi, E. B., J. Péduzzi, M. Barthélémy, and R. Labia. 1997. Are TEM β-lactamases encoded by pBR322 and Bluescript plasmids enzymatically indistinguishable? J. Antimicrob. Chemother. 39:668-669.
    • (1997) J. Antimicrob. Chemother. , vol.39 , pp. 668-669
    • Chaibi, E.B.1    Péduzzi, J.2    Barthélémy, M.3    Labia, R.4
  • 9
    • 0345055311 scopus 로고    scopus 로고
    • Clinical inhibitor-resistant mutants of the β-lactamase TEM-1 at amino-acid position 69. Kinetic analysis and molecular modelling. Biochim
    • Chaibi, E. B., J. Péduzzi, S. Farzaneh, M. Barthélémy, D. Sirot, and R. Labia. 1998. Clinical inhibitor-resistant mutants of the β-lactamase TEM-1 at amino-acid position 69. Kinetic analysis and molecular modelling. Biochim. Biophys. Acta 1382:38-46.
    • (1998) Biophys. Acta , vol.1382 , pp. 38-46
    • Chaibi, E.B.1    Péduzzi, J.2    Farzaneh, S.3    Barthélémy, M.4    Sirot, D.5    Labia, R.6
  • 10
    • 0026779284 scopus 로고
    • Site-directed mutagenesis at the active site of Escherichia coli TEM-1 β-lactamase. Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in catalysis
    • Delaire, M., R. Labia, J. P. Samama, and J. M. Masson. 1992. Site-directed mutagenesis at the active site of Escherichia coli TEM-1 β-lactamase. Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in catalysis, J. Biol. Chem. 267:20600-20606.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20600-20606
    • Delaire, M.1    Labia, R.2    Samama, J.P.3    Masson, J.M.4
  • 12
    • 0031960128 scopus 로고    scopus 로고
    • Properties of mutant SHV-5 β-lactamases constructed by substitution of isoleucine or valine for methionine at position 69
    • Giakkoup, P., V. Miriagou, M. Gazouli, E. Tzelepi, N. J. Legakis, and L. S. Tzouvelekis. 1998. Properties of mutant SHV-5 β-lactamases constructed by substitution of isoleucine or valine for methionine at position 69. Antimicrob. Agents Chemother. 42:1281-1283.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1281-1283
    • Giakkoup, P.1    Miriagou, V.2    Gazouli, M.3    Tzelepi, E.4    Legakis, N.J.5    Tzouvelekis, L.S.6
  • 13
    • 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
  • 14
    • 0027316253 scopus 로고
    • Inactivation of class A β-lactamases by clavulanic acid: The role of arginine-244 in a proposed nonconcerted sequence of events
    • Imtiaz, U., E. 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 proposed nonconcerted 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.2    Knox, J.R.3    Manavathu, E.K.4    Lerner, S.A.5    Mobashery, S.6
  • 15
    • 0028222371 scopus 로고
    • Reversal of clavulanate resistance conferred by a Ser-244 mutant of TEM-1 β-lactamase as a result of a second mutation (Arg to Ser at position 164) that enhances activity against ceftazidime
    • Imtiaz, U., E. K. Manavathu, S. Mobashery, and S. A. Lerner. 1994. Reversal of clavulanate resistance conferred by a Ser-244 mutant of TEM-1 β-lactamase as a result of a second mutation (Arg to Ser at position 164) that enhances activity against ceftazidime. Antimicrob. Agents Chemother. 38: 1134-1139.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1134-1139
    • Imtiaz, U.1    Manavathu, E.K.2    Mobashery, S.3    Lerner, S.A.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
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zkour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zkour, R.A.3
  • 18
    • 0028883511 scopus 로고
    • β-Lactamases in laboratory and clinical resistance
    • Livermore, D. M. 1995. β-Lactamases in laboratory and clinical resistance. Clin. Microbiol. Rev. 8:557-584.
    • (1995) Clin. Microbiol. Rev. , vol.8 , pp. 557-584
    • Livermore, D.M.1
  • 19
    • 0032032930 scopus 로고    scopus 로고
    • Catalytic properties of class A β-lactamases: Efficiency and diversity
    • Matagne, A., J. Lamotte-Brasseur, and J.-M. Frére. 1998. Catalytic properties of class A β-lactamases: efficiency and diversity. Biochem. J. 330:581-598.
    • (1998) Biochem. J. , vol.330 , pp. 581-598
    • Matagne, A.1    Lamotte-Brasseur, J.2    Frére, J.-M.3
  • 20
    • 23444456920 scopus 로고
    • Prevention of drug access to bacterial targets: Permeability barriers and active efflux
    • Nikaido, H. 1994. Prevention of drug access to bacterial targets: permeability barriers and active efflux. Science 264:382-388.
    • (1994) Science , vol.264 , pp. 382-388
    • Nikaido, H.1
  • 21
    • 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. Swarén, F. Lefèvre, J.-M. Masson, J.-C. Promé, 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    Swarén, P.3    Lefèvre, F.4    Masson, J.-M.5    Promé, J.-C.6    Samama, J.-P.7
  • 22
    • 0031009295 scopus 로고    scopus 로고
    • A complex mutant of TEM-1 β-lactamase with mutations encountered in both IRT-4 and extended-spectrum TEM-15, produced by an Escherichia coli clinical isolate
    • Sirot, D., C. Recule, E. B. Cbaibi, L. Bret, J. Croize, C. Chanal-Claris, R. Labia, and J. Sirot. 1997. A complex mutant of TEM-1 β-lactamase with mutations encountered in both IRT-4 and extended-spectrum TEM-15, produced by an Escherichia coli clinical isolate. Antimicrob. Agents Chemother. 41:1322-1325.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1322-1325
    • Sirot, D.1    Recule, C.2    Cbaibi, E.B.3    Bret, L.4    Croize, J.5    Chanal-Claris, C.6    Labia, R.7    Sirot, J.8
  • 23
    • 0025806002 scopus 로고
    • Substitution of lysine at position 104 or 240 of TEM-1pTZ18R β-lactamase enhances the effect of serine-164 substitution on hydrolysis or affinity for cephalosporins and the monobactam aztreonam
    • Sowek, J. A., S. B. Singer, S. Ohringer, M. F. Malley, T. J. Dougherty, J. Z. Gougoutas, and K. Bush. 1991. Substitution of lysine at position 104 or 240 of TEM-1pTZ18R β-lactamase enhances the effect of serine-164 substitution on hydrolysis or affinity for cephalosporins and the monobactam aztreonam. Biochemistry 30:3179-3188.
    • (1991) Biochemistry , vol.30 , pp. 3179-3188
    • Sowek, J.A.1    Singer, S.B.2    Ohringer, S.3    Malley, M.F.4    Dougherty, T.J.5    Gougoutas, J.Z.6    Bush, K.7
  • 24
    • 0028420272 scopus 로고
    • Resistance to antibiotics mediated by target alterations
    • Spratt, B. G. 1994. Resistance to antibiotics mediated by target alterations. Science 265:388-393.
    • (1994) Science , vol.265 , pp. 388-393
    • Spratt, B.G.1
  • 25
    • 0028840293 scopus 로고
    • The ability of β-lactam antibiotics to select mutants with derepressed β-lactamase synthesis from Citrobacter freundii
    • Stapleton, P., K. Shannon, and I. Phillips. 1995. The ability of β-lactam antibiotics to select mutants with derepressed β-lactamase synthesis from Citrobacter freundii. J. Antimicrob. Chemother. 36:483-496.
    • (1995) J. Antimicrob. Chemother. , vol.36 , pp. 483-496
    • Stapleton, P.1    Shannon, K.2    Phillips, I.3
  • 26
    • 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. 39:2479-2483.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2479-2483
    • Stapleton, P.1    P-J, W.2    King, A.3    Shannon, K.4    French, G.5    Phillips, I.6
  • 28
    • 0000845013 scopus 로고
    • Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322
    • Sutcliffe, J. G. 1978. Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322. Proc. Natl. Acad. Sci. USA 75:3737-3741.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3737-3741
    • Sutcliffe, J.G.1
  • 29
    • 0031834415 scopus 로고    scopus 로고
    • Selection and characterization of β-lactam-β-lactamase inactivator-resistant mutants following PCR mutagenesis of the TEM-1 β-lactamase gene
    • Vakulenko, S. B., B. Geryk, L. P. Kotra, S. Mobashery, and S. A. Lerner. 1998. Selection and characterization of β-lactam-β-lactamase inactivator-resistant mutants following PCR mutagenesis of the TEM-1 β-lactamase gene. Antimicrob. Agents Chemother. 42:1542-1548.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1542-1548
    • Vakulenko, S.B.1    Geryk, B.2    Kotra, L.P.3    Mobashery, S.4    Lerner, S.A.5
  • 30
    • 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, R. Labia, A. Philippon, P. Névot, 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    Labia, R.4    Philippon, A.5    Névot, P.6    Paul, G.7
  • 31
    • 0026654218 scopus 로고
    • Elucidation of the role of arginine-244 in the turnover processes 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 processes 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
  • 32
    • 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


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