Molecular and biochemical characterization of a carbapenem-hydrolysing β-lactamase from Flavobacterium johnsoniae

Journal of Antimicrobial Chemotherapy

Volumn 51, Issue 2, 2003, Pages 267-273

  Naas, Thierry ^a   Bellais, Samuel ^a   Nordmann, Patrice ^a  

^a BICÊTRE HOSPITAL   (France)

Author keywords

Carbapenem; Class B lactamase; Flavobacterium johnsoniae

Indexed keywords

AMOXICILLIN; AZTREONAM; BACTERIAL ENZYME; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CARBAPENEM; CARBAPENEM DERIVATIVE; CEFALOTIN; CEFEPIME; CEFOTAXIME; CEFOXITIN; CEFPIROME; CEFTAZIDIME; CEFTRIAXONE; CEPHALOSPORIN DERIVATIVE; CLAVULANIC ACID; IMIPENEM; LATAMOXEF; MEROPENEM; METALLOPROTEINASE; MONOBACTAM DERIVATIVE; MONOMER; PENICILLIN DERIVATIVE; PIPERACILLIN; TICARCILLIN; ZINC;

AMINO ACID SEQUENCE; ANTIBIOTIC RESISTANCE; BACTERIAL GENE; CHRYSEOBACTERIUM; CHRYSEOBACTERIUM INDOLOGENES; CHRYSEOBACTERIUM MENINGOSEPTICUM; CONTROLLED STUDY; DRUG HYDROLYSIS; DRUG SENSITIVITY; ENZYME KINETICS; ENZYME PURIFICATION; ESCHERICHIA COLI; FLAVOBACTERIUM JOHNSONIAE; GENE EXPRESSION; GENETIC HETEROGENEITY; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYLOGENY; REVIEW; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BETA-LACTAMASES; CARBAPENEMS; DNA, BACTERIAL; ESCHERICHIA COLI; FLAVOBACTERIUM; ISOENZYMES; KINETICS; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT;

EID: 0037323917     PISSN: 03057453     EISSN: None     Source Type: Journal    
DOI: 10.1093/jac/dkg069     Document Type: Review

References (33)

1. Bush, K. (1998). Metallo-β-lactamases: a class apart. Clinical Infectious Diseases 27, S48-53.
2. Walsh, T. R., Hall, L., Assinder, S. J., Nichols, W. W., Cartwright, S. J., MacGowan, A. P. et al. (1994). Sequence analysis of the L-1 metallo β-lactamase from Xanthomonas maltophilia. Biochimica Biophysica Acta 1218, 199-201.
3. Lim, H. M., Pene, J. J. & Shaw, R. (1988). Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 β-lactamase II structural gene. Journal of Bacteriology 170, 2873-8.
4. Podglajen, I., Breuil, J., Casin, I. & Collatz, E. (1995). Genotypic identification of two groups within the species Bacteroides fragilis by ribotyping and by analysis of PCR-generated fragment patterns and insertion sequence content. Journal of Bacteriology 177, 5270-5.
5. Rasmussen, B. A., Gluzman, Y. & Tally, F. P. (1990). Cloning and sequencing of the class B β-lactamase gene (ccrA) from Bacteroides fragilis TAL3636. Antimicrobial Agents and Chemotherapy 34, 1590-2.
6. Massidda, O., Rossolini, G. M. & Satta, G. (1991). The Aeromonas hydrophila cphA gene: molecular heterogeneity among metallo-β-lactamases. Journal of Bacteriology 173, 4611-7.
7. Boschi, L., Mercuri, P. S., Riccio, M. L., Amicosante, G., Galleni, M., Frère, J.-M. et al. (2000). The Legionella (Fluoribacter) gormanii metallo-β-lactamase: a new member of the high divergent lineage of molecular subclass B3 β-lactamases. Antimicrobial Agents and Chemotherapy 44, 1538-43.
8. Rossolini, G. M., Condemi, M. A., Pantanella, F., Docquier, J. D., Amicosante, G. & Thaller, M. C. (2001). Metallo-β-lactamase producers in environmental microbiota: new molecular class B enzyme in Janthinobacterium lividum. Antimicrobial Agents and Chemotherapy 45, 837-44.
9. Bellais, S., Aubert, D., Naas, T. & Nordmann, P. (2000). Molecular and biochemical heterogeneity of class B carbapenem-hydrolyzing β-lactamases in Chryseobacterium meningosepticum. Antimicrobial Agents and Chemotherapy 44, 1878-86.
10. Bellais, S., Léotard, S., Poirel, L., Naas, T. & Nordmann, P. (1999). Molecular characterization of a carbapenem-hydrolyzing β-lactamase from Chryseobacterium (Flavobacterium) indologenes. FEMS Microbiology Letters 171, 127-32.
11. Bellais, S., Poirel, L., Léotard, S., Naas, T. & Nordmann, P. (2000). Genetic diversity of carbapenem-hydrolyzing metallo-beta-lactamases from Chryseobacterium (Flavobacterium) indologenes. Antimicrobial Agents and Chemotherapy 44, 3028-34.
12. Rossolini, G. M., Franceschini, N., Riccio, M. L., Mercuri, P. S., Perilli, M., Galleni, M. et al. (1998). Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B β-lactamase showing a broad substrate profile. Biochemical Journal 332, 145-52.
13. VIM, a new integron-borne metallo-β-lactamase gene from a Pseudomonas aeruginosa clinical isolate. Antimicrobial Agents and Chemotherapy 43, 1584-90.
14. IMP. Antimicrobial Agents and Chemotherapy 39, 1612-5.
15. Bernardet, J. F., Segers, P., Vancanneyt, M., Berthe, F., Kersters, K. & Vandamme, P. (1996). Cutting a gordian knot: amended classification and description of the genus Flavobacterium, amended description of the family Flavobacteriaceae, and proposal of Flavobacterium hydatis nom. nov. (Basonym, Cytophaga aquatilis Strohl and Tait 1978). International Journal of Systematic Bacteriology 46, 128-48.
16. Carson, J., Schmidtke, L. M. & Munday, B. L. (1993). Cytophaga johnsonae: a putative skin pathogen of juvenile farmed barramunid, Later calcarifer Bloch. Journal of Fishery Diseases 16, 209-18.
17. Lednicka, D., Mergaert, J., Cnockaert, M. C. & Swings, J. (2000). Isolation and identification of cellulolytic bacteria involved in the degradation of natural cellulosic fibres. Systematic and Applied Microbiology 23, 292-9.
18. Poirel, L., Naas, T., Guibert, M., Chaibi, E. B., Labia, R. & Nordmann, P. (1999). Molecular and biochemical characterization of VEB-1, a novel class A extended-spectrum β-lactamase encoded by an Escherichia coli integron gene. Antimicrobial Agents and Chemotherapy 43, 573-81.
19. National Committee for Clinical Laboratory Standards. (2001). Methods for Dilution Antimicrobial Susceptibility Tests for Bacteria that Grow Aerobically: Approved Standard M7-A5. NCCLS, Wayne, PA, USA.
20. Naas, T., Blot, M., Fitch, W. M. & Arber, W. (1994). Insertion sequence-related genetic variation in resting Escherichia coli K-12. Genetics 136, 721-30.
21. Nordmann, P. & Naas, T. (1994). Sequence analysis of PER-1 extended-spectrum beta-lactamase from Pseudomonas aeruginosa and comparison with class A β-lactamases. Antimicrobial Agents and Chemotherapy 38, 104-14.
22. Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA.
23. Naas, T., Sougakoff, W., Casetta, A. & Nordmann, P. (1998). Molecular characterization of OXA-20, a novel class D β-lactamase, and its integron from Pseudomonas aeruginosa. Antimicrobial Agents and Chemotherapy 42, 2074-83.
24. Nielsen, H., Engelbrecht, J., Brunak, S. & Von Heijne, G. (1997). A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. International Journal of Neurology and Systematics 8, 581-99.
25. Galleni, M., Lamotte-Brasseur, J., Rossolini, G. M., Spencer, J., Dideberg., O. & Frère, J.-M. (2001). Standard numbering scheme for class B beta-lactamases. Antimicrobial Agents and Chemotherapy 45, 660-3.
26. Hunnicutt, D. W. & McBride, M. J. (2001). Cloning and characterization of the Flavobacterium johnsoniae gliding motility genes gldD and gldE. Journal of Bacteriology 183, 4167-75.
27. Rasmussen, B. A. & Bush, K. (1997). Carbapenem-hydrolyzing β-lactamases. Antimicrobial Agents and Chemotherapy 41, 223-32.
28. Mazel, D., Coic, E., Blanchard, S., Saurin, W. & Marliere, P. (1997). A survey of polypeptide deformylase function throughout the eubacterial lineage. Journal of Molecular Biology 266, 939-49.
29. Blattner, F. R., Burland, V., Plunkett, G., Sofia, H. J. & Daniels, D. L. (1993). Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 min. Nucleic Acids Research 21, 5408-17.
30. Overhage, J., Kresse, A. U., Priefert, H., Sommer, H., Krammer, G., Rabenhorst, J. et al. (1999). Molecular characterization of the genes pcaG and pcaH, encoding protocatechuate 3,4-dioxygenase, which are essential for vanillin catabolism in Pseudomonas sp. strain HR199. Applied and Environmental Microbiology 65, 951-60.
31. Carfi, A., Duée, E., Galleni, M., Frère, J.-M. & Dideberg, O. (1998). 1.85 Å resolution structure of the Zn(II) β-lactamase from Bacillus cereus. Acta Crystallographica D 54, 313-23.
32. Concha, N. O., Rasmussen, B. A., Bush, K. & Herzberg, O. (1996). Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis. Structure 4, 823-36.
33. Wang, Z., Fast, W., Valentine, A. M. & Benkovic, S. J. (1999). Metallo-β-lactamase: structure and mechanism. Current Opinion in Chemical Biology 3, 614-22.