An extended-spectrum AmpC-type β-lactamase obtained by in vitro antibiotic selection

FEMS Microbiology Letters

Volumn 165, Issue 1, 1998, Pages 85-90

  Morosini, María Isabel ^a   Negri, María Cristina ^a   Shoichet, Brian ^b   Baquero, María Rosario ^a   Baquero, Fernando ^a   Blázquez, Jesús ^a  

^a HOSPITAL RAMÓN Y CAJAL   (Spain)

^b NORTHWESTERN UNIVERSITY   (United States)

Author keywords

Lactamase; AmpC mutant; Cephem resistance; Evolution of resistance

Indexed keywords

AMOXICILLIN; AMOXICILLIN PLUS CLAVULANIC ACID; BETA LACTAMASE; CEFEPIME; CEFOTAXIME; CEFOXITIN; CEFPIROME; CEFTAZIDIME; CEPHALOSPORIN; CEPHEM DERIVATIVE; CLAVULANIC ACID; IMIPENEM; MEROPENEM; PENICILLIN DERIVATIVE; PIPERACILLIN; PIPERACILLIN PLUS TAZOBACTAM; TAZOBACTAM;

ANTIBIOTIC RESISTANCE; ANTIBIOTIC SENSITIVITY; ARTICLE; ESCHERICHIA COLI; GENE EXPRESSION; IN VITRO STUDY; MINIMUM INHIBITORY CONCENTRATION; MOLECULAR CLONING; MUTANT; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; BETA-LACTAM RESISTANCE; BETA-LACTAMASES; CEPHALOSPORINS; CLONING, MOLECULAR; ENTEROBACTER CLOACAE; GENES, BACTERIAL; MOLECULAR SEQUENCE DATA; MUTATION; PENICILLINS; PHENOTYPE;

ENTEROBACTER CLOACAE;

EID: 0032146144     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(98)00239-0     Document Type: Article

References (18)

1. Bush, K., Jacoby, G.A. and Medeiros, A.A. (1995) A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39, 1211-1233.
2. Tuomanen, E., Lindquist, S., Sande, S., Galleni, M., Light, K., Gage, D. and Normark, S. (1991) Coordinate regulation of β-lactamase induction and peptidoglycan composition by the amp operon. Science 251, 201-204.
3. 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.
4. Galleni, M., Lindberg, F., Normark, S., Cole, S., Honoré, N., Joris, B. and Frère, J.M. (1988) Sequence and comparative analysis of three Enterobacter cloacae ampC β-lactamase genes and their products. Biochem. J. 250, 753-760.
5. González-Leiza, M., Pérez-Díaz, J.C., Ayala, J., Casellas, J.M., Martínez-Beltrán, J., Bush, K. and Baquero, F. (1994) Gene sequence and biochemical characterization of FOX-1 from Klebsiella pneumoniae, a new AmpC-type plasmid-mediated β-lactamase with two molecular variants. Antimicrob. Agents Chemother. 38, 2150-2157.
6. MOX-1 gene encoding AmpC type-β-lactamase. Gene 139, 93-98.
7. Gaillot, O., Clément, C., Simonet, M. and Philippon, A. (1997) Novel transferable β-lactam resistance with cephalosporinase characteristics in Salmonella enteritidis. J. Antimicrob. Chemother. 39, 85-87.
8. Koeck, J.L., Arlet, G., Philippon, A., Basmaciogullari, S., Thien, H.V., Buisson, Y. and Cavallo, J.D. (1997) A plasmid-mediated CMY-2 β-lactamase from an algerian clinical isolate of Salmonella senftenberg. FEMS Microbiol. Lett. 152, 255-260.
9. Spratt, B.G., Hedge, P.I., Heesen, S., Edelman, A. and Broome-Smith, J.K. (1986) Kanamycin-resistant vectors that are analogs of plasmids pUC8, pUC9, pEMBL8, and pEMBL9. Gene 41, 337-342.
10. Condon, C. and Weiner, J.H. (1988) Fumarate reductase of Escherichia coli: an investigation of function and assembly using in vivo complementation. Mol. Microbiol. 2, 43-52.
11. Dao-Pin, S., Anderson, D.E., Baase, W.A., Dahlquist, F.W. and Matthews, B.W. (1991) Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. Biochemistry 30, 11521-11529.
12. Shoichet, B.K., Baase, W.A., Kuroki, R. and Matthews, B.W. (1995) A relationship between protein stability and protein function. Proc. Natl. Acad. Sci USA 92, 452-456.
13. Rose, R.B., Craik, C.S. and Stroud, R.M. (19??) Domain flexibility in retroviral proteases: structural implications for drug resistant mutations. Biochemistry 37, 2607-2621.
14. Lindberg, F., Lindquist, S. and Normark, S. (1986) Induction of chromosomal β-lactamase expression in enterobacteria. J. Antimicrob. Chemother. 18, Suppl. C, 43-50.
15. Garau, J., Wilson, W., Wood, M. and Carlet, J. (1997) Fourth-generation cephalosporins: a review of in vitro activity, pharmacokinetics, pharmacodynamics and clinical utility. Clin. Microbiol. Infect. 13, Suppl. 1, 87-101.
16. Sanders, W.E. Jr., Tenney, J.H. and Kessler, R.E. (1996) Efficacy of cefepime in the treatment of infections due to multiply resistant Enterobacter species. Clin. Infect. Dis. 23, 454-461.
17. Segreti, J. and Levin, S. (1996) Bacteriologic and clinical applications of a new-spectrum parenteral cephalosporin. Am. J. Med. 100, 45S-51S.
18. Ferrin, T.E., Huang, C.C., Jarvis, L.E. and Langridge, R. (1988) The MIDAS display system. J. Mol. Graph. 6, 13-27.