The Legionella (Fluoribacter) gormanii metallo-β-lactamase: A new member of the highly divergent lineage of molecular-subclass B3 β-lactamases

Antimicrobial Agents and Chemotherapy

Volumn 44, Issue 6, 2000, Pages 1538-1543

  Boschi, Letizia ^a   Mercuri, Paola Sandra ^b   Riccio, Maria Letizia ^a   Amicosante, Gianfranco ^c   Galleni, Moreno ^b   Frère, Jean Marie ^b   Rossolini, Gian Maria ^a  

^a UNIVERSITY OF SIENA   (Italy)

^b UNIVERSITY OF LIÈGE   (Belgium)

^c Universit de l'Aquila   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

AZTREONAM; BETA LACTAMASE; CEFOTAXIME; CEFOXITIN; CEFTAZIDIME; CEFUROXIME; CEPHALOSPORIN DERIVATIVE; DNA; IMIPENEM; MEROPENEM; NITROCEFIN; POLYPEPTIDE; ZINC;

ANTIBIOTIC SENSITIVITY; ARTICLE; DNA SEQUENCE; ENZYME SPECIFICITY; GEL PERMEATION CHROMATOGRAPHY; GENE; GENE EXPRESSION; LEGIONELLA; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; BASE SEQUENCE; BETA-LACTAMASES; CLONING, MOLECULAR; GENES, BACTERIAL; LEGIONELLA; MOLECULAR SEQUENCE DATA; SEQUENCE ALIGNMENT;

EID: 0034128893     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.44.6.1538-1543.2000     Document Type: Article

References (33)

1. Altschul, S. F., T. L. Madden, A. A. Schaffer, J. Zhang, Z. Zhang, W. Miller, and D. J. Lipman. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389-3402.
2. IMP. Antimicrob. Agents Chemother. 39: 1612-1615.
3. Baxter, I. A., and P. A. Lambert. 1994. Isolation and partial purification of a carbapenem-hydrolysing metallo-β-lactamase from Pseudomonas cepacia. FEMS Microbiol. Lett. 122:251-256.
4. Bellais, S., S. Leotard, L. Poirel, T. Naas, and P. Nordmann. 1999. Molecular characterization of a carbapenem-hydrolysing β-lactamase from Chryseobacterium (Flavobacterium) indologenes. FEMS Microbiol. Lett. 171:127-132.
5. Brenner, D. J., J. C. Feeley, and R. E. Weaver. 1984. Family VII. Legionellaceae, p. 279. In N. R. Krieg and J. G. Holt (ed.), Bergey's manual of systematic bacteriology, vol. 1. The William & Wilkins Co., Baltimore, Md.
6. Bush, K. 1998. Metallo-β-lactamases: a class apart. Clin. Infect. Dis. 27:S48-S53.
7. 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.
8. Carfi, A., E. Duée, M. Galleni, J.-M. Frère, and O. Dideberg. 1998. 1.85 Å resolution structure of the zinc(II) β-lactamase from B cereus. Acta Crystallog. Sect. D 54:313-323.
9. Carfi, A., S. Pares, E. Duée, M. Galleni, C. Duez, J.-M. Frère, and O. Dideberg. 1995. The 3-D structure of a zinc metalio-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14:4914-4921.
10. Chang, A. C., and S. N. Cohen. 1978. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J. Bacteriol. 134:1141-1156.
11. Concha, N., B. A. Rasmussen, K. Bush, and O. Herzberg. 1996. Crystal structure of the wide-spectrum binuclcar zinc β-lactamase from Bacteroides fragilis. Structure 4:823-836.
12. Felici, A., G. Amicosante, A. Oratore, R. Strom, P. Ledent, B. Joris, L. Fanuel, and J.-M. Frère. 1993. An overview of the kinetic parameters of class B β-Jactamases. Biochem. J. 291:151-155.
13. Frère, J. M. 1995. Beta-lactamases and bacterial resistance to antibiotics. Mol. Microbiol. 16:385-395.
14. Fujii, T., K. Sato, K. Miyata, M. Inoue, and S. Mitsuhashi. 1986. Biochemical properties of β-lactamase produced by Legionella gonnunii. Antimicrob. Agents Chemother. 29:925-926.
15. Hussain, M., A. Carlino, M. J. Madonna, and J. O. Lampen. 1985. Cloning and sequencing of the metallothioprotein β-lactamase II gene of Bacillus cereus 569/H in Escherichia coli. J. Bacteriol. 164:223-229.
16. Johnson, J. L. 1994. Similarity analysis of DNAs, p. 655-682. In P. Gerhardt, R. G. E. Murray, W. A. Wood, and N. R. Krieg (ed.), Methods for general and molecular bacteriology American Society for Microbiology, Washington, D.C.
17. IMP-containing Pseudomonas aeruginosa integron phyletically related to In5, which carries an unusual array of gene cassettes. Antimicrob. Agents Chemother. 43:890-901.
18. VIM, a new integron-borne metallo-β-lactamase gene from a Pseudomonus aeruginosa clinical isolate. Antimicrob. Agents Chemother. 43:1584-1590.
19. Livermore, D. M. 1995. β-Lactamases in laboratory and clinical resistance. Clin. Microbiol. Rev. 8:557-584.
20. Livermore, D. M., and J. D. Williams. 1996. β-Lactams: mode of action and mechanisms of bacterial resistance, p. 502-578. In V. Lorian (ed.), Antibiotics in laboratory medicine, 4th ed. The William & Wilkins Co., Baltimore, Md.
21. Massidda, O., G. M. Rossolini, and G. Satta. 1991. The Aeromonas hydrophyla cphA gene: molecular heterogeneity among metallo-β-lactamases. J. Bacteriol. 173:4611-4617.
22. National Committee for Clinical Laboratory Standards. 1997. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically, 4th ed. Approved standard. NCCLS document M7-A4. National Committee for Clinical Laboratory Standards. Wayne, Pa.
23. Osano, E., Y. Arakawa, R. Wacharotayankun, M. Ohta, T. Horii, H. Ito, F. Yoshimura, and N. Kato. 1994, Molecular characterization of an enterobacterial metallo-β-lactamase found in a clinical isolate of Serrtia marcescens that shows imipenem resistance. Antimicrob. Agents Chemother. 38:71-78.
24. Pugsley, A. P. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50-108.
25. Rasmussen, B. A., Y. Gluzman, and F. P. Tally. 1990. Cloning and sequencing of the class B β-lactamase gene (ccrA) from Bacteroides fragilis TAL3636. Antimicrnb. Agents Chemother. 34:1590-1592.
26. Rasmussen, B. A., and K. Bush. 1997. Carbapenem-hydrolyzing β-lactamases. Antimicrob. Agents Chemother. 41:223-232.
27. Rossolini, G. M., N. Franceschini, M. L. Riccio, P. S. Mercuri, M. Perilli, M. Galleni, J.-M. Frère, and G. Amicosante. 1998 Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B β-lactamase showing a broad substrate profile. Biochem. J. 332:145-152.
28. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N. Y.
29. Sanschagrin, F., J. Dufresne, and R. C. Levesque. 1998. Molecular heterogeneity of the L-1 metallo-β-lactamase family from Stenotrophomonas maltophilia. Antimicrob. Agents Chemother. 42:1245-1248.
30. Sato, K., T. Fujii, R. Okamoto, M. Inoue, and S. Mitsuhashi. 1985. Biochemical properties of β-lactamase produced by Flavobacterium odoratum. Antimicrob. Agents Chemother. 27:612-614.
31. Ullah, J. H., T. R. Walsh, I. A. Taylor, D. C. Emery, C. S. Verma, S. J. Gamblin, and J. Spencer. 1998. The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas multophilia at 1.7 Å resolution. J. Mol. Biol. 284:125-136.
32. Walsh, T. R., L. Hall, S. J. Assinder, W. W. Nichols, S. J. Cartwright, A. P. MacGowan, and P. M. Bennet. 1994. Sequence analysis of the L1 metallo-β-lactamase from Xanthotnonas mahophilia. Biochim. Biophys. Acta 1218: 199-201.
33. Walsh, T. R., W. A. Neville, M. H. Haran, D. Tolson, D. J. Payne, J. H. Bateson, A. P. MacGowan, and P. M. Bennett. 1998. Nucleotide and amino acid sequences of the metallo-β-lactamase, ImiS, from Aeromonas veronii bv. sobria. Antimicrob. Agents Chemother. 42:436-439.