Identification of putative zinc hydrolase genes of the metallo-β- lactamase superfamily from Campylobacter jejuni

FEMS Immunology and Medical Microbiology

Volumn 49, Issue 1, 2007, Pages 159-164

  Alfredson, David A ^a   Korolik, Victoria ^a  

^a GRIFFITH UNIVERSITY   (Australia)

Author keywords

Campylobacter; Metallo lactamase; Zinc hydrolase

Indexed keywords

BACTERIAL ENZYME; METALLO BETA LACTAMASE; UNCLASSIFIED DRUG; ZINC HYDROLASE;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; BACTERIAL STRAIN; BACTERIUM ISOLATE; CAMPYLOBACTER JEJUNI; CONTROLLED STUDY; GENE IDENTIFICATION; GENE SEQUENCE; GENETIC CONSERVATION; LIGAND BINDING; METAL BINDING; MOLECULAR CLONING; MULTIGENE FAMILY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BASE SEQUENCE; BETA-LACTAMASES; CAMPYLOBACTER JEJUNI; HUMANS; MOLECULAR SEQUENCE DATA; THIOLESTER HYDROLASES; ZINC;

EID: 33846557280     PISSN: 09288244     EISSN: 1574695X     Source Type: Journal    
DOI: 10.1111/j.1574-695X.2006.00197.x     Document Type: Article

References (27)

1. Alfredson D & Korolik V (2003) Sequence analysis of a cryptic plasmid pCJ419 from Campylobacter jejuni and construction of an Escherichia coli-Campylobacter shuttle vector. Plasmid 50: 152-160.
2. Alfredson D & Korolik V (2005) Isolation and expression of a novel class D β-lactamase, OXA-61, from Campylobacter jejuni. Antimicrob Agents Chemother 49: 2515-2518.
3. Alfredson D, Akhurst RJ & Korolik V (2003) Antimicrobial resistance and genomic screening of clinical isolates of thermophilic Campylobacter spp. from south-east Queensland, Australia. J Appl Microbiol 94: 495-500.
4. Altschul SF, Maden TL, Schaffer AA, Zhang J, Zhang Z, Miller W & Lipman DJ (1997) Gapped BLAST and PSI-BLAST: a new generation of protein data-base search programs. Nucleic Acids Res 25: 3389-3402.
5. Blaser MJ (1997) Epidemiological and clinical features of Campylobacter jejuni infections. J Infect Dis 176 (Suppl 2), S103-S105.
6. Bush K, Jacoby G & Medeiros A (1995) A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob Agents Chemother 39: 1211-1233.
7. Daiyasu H, Osaka K, Ishino Y & Toh H (2001) Expansion of the zinc metallo-hydrolase family of the β-lactamase fold. FEBS Lett 503: 1-6.
8. Galleni M, Lamotte-Brasseur J, Rossolini GM, Spencer J, Dideberg O & Frere J-MThe Metallo β-Lactamase Working Group (2001) Standard numbering scheme for class B β-lactamases. Antimicrob Agents Chemother 45: 660-663.
9. Gomes CM, Frazao C, Xavier AV, Legall J & Teixeira M (2002) Functional control of the binuclear metal site in the metallo-β-lactamase- like fold by subtle amino acid replacements. Protein Sci 11: 707-712.
10. Hall BG, Salipante SJ & Barlow M (2003) The metallo-β-lactamases fall into two distinct phylogenetic groups. J Mol Evol 57: 249-254.
11. Lachance N, Gaudreau C, Lamothe F & Lariviere L (1991) Role of β-lactamase of Campylobacter jejuni in resistance to β-lactam agents. Antimicrob Agents Chemother 35: 813-818.
12. Lachance N, Gaudreau C, Lamothe F & Turgeon F (1993) Susceptibilities of β-lactamase-positive and -negative strains of Campylobacter coli to β-lactam agents. Antimicrob Agents Chemother 37: 1174-1176.
13. Livermore D & Woodford N (2000) Carbapenemases: a problem in waiting? Curr Opin Microbiol 3: 489-495.
14. Melino S, Capo C, Dragani B, Azeto A & Petruzzelli R (1998) A zinc-binding motif conserved in glyoxalase II, β-lactamase and arylsulfatases. Trends Biochem Sci 23: 381-382.
15. National Committee for Clinical Laboratory Standards (2003) Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically. Approved Standard M7-A6. National Committee for Clinical Laboratory Standards, Wayne, PA.
16. Nordmann P & Poirel L (2002) Emerging carbapenemases in Gram-negative aerobes. Clin Microbiol Infect 8: 321-331.
17. Parkhill J, Wren BW, Mungall K et al. (2000) The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences. Nature 403: 665-668.
18. Rasmussen BA & Bush K (1997) Carbapenem-hydrolyzing beta-lactamases. Antimicrob Agents Chemother 41: 223-232.
19. Schilling O, Wenzel N, Naylor M, Vogel A, Crowder M, Makaroff C & Meyer-Klaucke W (2003) Flexible metal binding of the metallo-β-lactamase domain: glyoxalase II incorporates iron, manganese, and zinc in vivo. Biochemistry 42: 11777-11786.
20. Tajada P, Gomez-Garces J-L, Alos J-I, Balas D & Cogollos R (1996) Antimicrobial susceptibilities of Campylobacter jejuni and Campylobacter coli to 12 β-lactam agents and combinations with β-lactamase inhibitors. Antimicrob Agents Chemother 40: 1924-1925.
21. Tremblay C & Gaudreau C (1998) Antimicrobial susceptibility testing of 59 strains of Campylobacter fetus subsp. fetus. Antimicrob Agents Chemother 42: 1847-1849.
22. Tremblay C, Gaudreau C & Lorange M (2003) Epidemiology and antimicrobial susceptibilities of 111 Campylobacter fetus subsp. fetus strains isolated in Quebec, Canada, from 1983 to 2000. J Clin Microbiol 41: 463-466.
23. Ullah JH, Walsh TR, Taylor IA, Emery DC, Verma CS, Gamblin SJ & Spencer J (1998) The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution. J Mol Biol 284: 125-136.
24. Wang Y & Taylor DE (1990) Natural transformation in Campylobacter species. J Bacteriol 172: 949-955.
25. Wenzel N, Carenbauer AL, Pfiester MP, Schilling O, Meyer-Klaucke W, Mackaroff CA & Crowder MW (2004) The binding of iron and zinc to glyoxalase II occurs exclusively as di-metal centers and is unique within the metallo-β-lactamase family. J Biol Inorg Chem 9: 429-438.
26. Wosten MMSM, Boeve M, Koot MGA, Van Nuenen AC & Van der Zeijst BAM (1998) Identification of Campylobacter jejuni promoter sequences. J Bacteriol 180: 594-599.
27. Zang T, Hollman DA, Crawford PA, Crowder MW & Makaroff CA (2001) Arabidopsis glyoxalase II contains a zinc/iron binuclear metal centre that is essential for substrate binding and catalysis. J Biol Chem 276: 4788-4795.