Identification of metallo-β-lactamase from a clinical isolate at Saint Camillle medical Center of Ouagadougou, Burkina Faso

African Journal of Biotechnology

Volumn 4, Issue 3, 2005, Pages 286-288

  Zeba, Boukaré ^a   Simporé, Pere Jacques ^b   Nacoulma, Odile G ^a   Frère, Jean Marie ^c  

^a UNIVERSITÉ DE OUAGADOUGOU   (Burkina Faso)

^b Centre Medical Saint Camille (CMSC)   (Burkina Faso)

^c Enzymology   (Belgium)

Author keywords

lactamase; Antibiotics; Bacterial resistance; Chyseobacterium indologenes; Metallo lactamase

Indexed keywords

AMPICILLIN; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CEFALOTIN; CEFOTAXIME; CEFUROXIME; IMIPENEM; PENICILLIN G;

ARTICLE; BACTERIAL STRAIN; BACTERIUM IDENTIFICATION; BACTERIUM ISOLATE; CHRYSEOBACTERIUM INDOLOGENES; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME SUBSTRATE; NONHUMAN;

BACTERIA (MICROORGANISMS); CHRYSEOBACTERIUM INDOLOGENES;

EID: 19244387488     PISSN: 16845315     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (14)

1. Ambler RP (1975). The aminoacid sequence of Staphylococcus aureus penicillinase .Biochem. J. 151 : 197-218.
2. Ambler RP, Scott G K.(1978). Partial aminoacid sequence of penici llinase coded by Escherichia coli plasmid R6K. Proc. Natl. Acad.Sci. USA 75 : 3732-3736.
3. Ambler RP (1980 ). The structure of β-lactamases. Philos.Trans. R. Soc. Lond. Ser. B. 289: 321-331.
4. Bellais S, Leotard S, Poirel L, Naas T, Nordmann P.(1999). Molecular characterization of carbapenem-hydrolysing β-lactamase from Chryseobacterium (Flavobactreium) indologenes. FEMS microbia .Letl. 171 : 127-132.
5. Bellais S, Poirel L, Leotard S, Naas T, Nordmann P (2000). Genetic diversity of carbapenem Hydrolyzing Metallo-β-lactamases from Chryseobacterium (Flavobacterium) indologenes. Antimicrob. Agents Chemother. 44: 1-9
6. B Bush K (1988). β-lactmamase inhibitors from laboratory to clinic. Clin. Microbiol. Rev.1: 109-123.
7. Bush K (1989). Characterization of β-lactamases. Antimicrob. Agents Chemother.33: 259-263.
8. Bush K (1989). Classification of β-lactamases: groups 1, 2a, 2b, and 2b'. Antimicrobial Agents and Chemother. pp. 264-270.
9. Bush K (1989). Classification of β-lactamases: groups 2c, 2d, 2e, 3, and 4. Antimicrob. Agents Chemother. 33: 271-276.
10. Concha NO, Rasmussen BA, Bush K, Herzberg O (1996). Crystal Structure of the IMP-1 Metallo-β-Lactamase from Pseudomonas aeruginosa and Its Complex with a Mercaptocarboxylate Inhibitor: Binding Determinants of a Potent, Broad-Spectrum Inhibitor. Structure 4: 823-836.
11. Orellano EG, Girardini JE, Cricco JA, Ceccarelli EA, Vila AJ (1998). Spectroscopic characterization of a binuclear metal site in Bacillus cereus β-lactamase II. Biochemistry 37: 10173-1018.
12. Rice LB, Carcias LL, Hujer AM, Bonafede M, Hutton R, Hoyen C, Bonomo RA (2000). High-Level expression of chromosomally encoded SHV-1 β-lactamase and an outer membrane protein change confer resistance to ceftazidime and piperacillin-tazobactan in clinical isolate of Klebsiella pneumoniae. Antimicrob. Agents Chemother. 44: 362-367.
13. Simpson IN, James M .(1982). Comparison of routine techniques for cell breakage and release of β-lactamase activity. Journal of Antimicrobial Chemother. 9: 119-123.
14. Woodford N, Paledou MFI, Babini GS, Holmes B, Livermore DM. (2000). Carbapenemase of Chryseobacterium ( Flavobacterium) meningosepticum: Distribution of blaB and characterization of a novel metallo-β-lactamase gene, BlaB3, in the type Strain, NCTC 10016. Antimicrob.Agents Chemother. 44: 1448-1452.