Resistance to β-Lactamines by Gram Negative Bacteria, Producing Several Types of Enzymes, Isolated from Urines in Pediatric Center of Ouagadougou in Burkina Faso
International Journal of Microbiology and Biotechnology
Volume 3, Issue 4, December 2018, Pages: 95-98
Received: Nov. 19, 2018;
Accepted: Dec. 5, 2018;
Published: Jan. 14, 2019
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Mètuor Dabiré Amana, Department of Biochemistry-Microbiology, University of Ouagadougou, Ouagadougou, Burkina Faso
Zongo Koudbi Jacob, Department of Biochemistry-Microbiology, University of Ouagadougou, Ouagadougou, Burkina Faso
Kaboré Boukaré, Department of Biochemistry-Microbiology, University of Ouagadougou, Ouagadougou, Burkina Faso
Zèba Boukaré, Department of Biochemistry-Microbiology, University of Ouagadougou, Ouagadougou, Burkina Faso
Baucher Marie, Department of Plant Biotechnology, Free University of Brussels, Brussels, Belgium
El Jaziri Mondher, Department of Plant Biotechnology, Free University of Brussels, Brussels, Belgium
Simporé Jacques, Department of Biochemistry-Microbiology, University of Ouagadougou, Ouagadougou, Burkina Faso
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Extended Spectrum β-Lactamases (ESBL) producing bacteria have been reported in several countries, but there is little information available on the different types of ESBL produced by Enterobacteria in Burkina Faso. For compensate for the lack of scientific information of extreme importance, this study deals with molecular characterization of several types of extended spectrum β-lactamases (ESBL) produced by Enterobacteria strains isolated in pediatric medium. Enterobacteria strains producing ESBL were identified by their profile of resistance to the cephalosporin of third generation (C3G) on Petri box. These strains consist of several bacterial species resistant to antibiotics. The production of ESBL by these strains was confirmed by kinetic approach. The genomes of the different strains were obtained by DNAZOL extraction. The molecular characterization of the ESBL was based on classical PCR and sequencing using specific primers of the CTX-M, SHV and TEM genes. CTX-M, SHV and TEM genes were searched in DNAs extracted from 30 isolates positives to ESBL production. CTX-M-15 was found in the 30 isolates, CTX-M-15 and SHV-1,-11,-12,-28,-32,-38,-76 or-99 in 11 isolates, CTX-M-15 and TEM-1 in 11 isolates , and CTX-M-15, TEM-1 and SHV-1,-11,-12,-32,- 76 or -99 in 5 isolates. β-lactamases types of CTX-M-15, TEM-1 and SHV-1,-11,-12,-28,-32,-38,-76 and-99 were highlighted in the University Hospital center Pediatric Charles De Gaulle of Ouagadougou/BF.
Extended Spectrum β-Lactamases, Genes, Resistance to Antibiotics
To cite this article
Mètuor Dabiré Amana,
Zongo Koudbi Jacob,
El Jaziri Mondher,
Resistance to β-Lactamines by Gram Negative Bacteria, Producing Several Types of Enzymes, Isolated from Urines in Pediatric Center of Ouagadougou in Burkina Faso, International Journal of Microbiology and Biotechnology.
Vol. 3, No. 4,
2018, pp. 95-98.
Copyright © 2018 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/
) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Philippon A, Arlet B, Jacoby GA. "Plasmid-determined AMPC-β-lactamases-type Antimicrob Agents Chemother, Prevalence and characterization of extended-spectrum cephalosporin-resistant non typhoidal Salmonella isolates in adults in Saint Petersburg, Russia (2002-2005). Microb Drug, Resist. Summe 2006; 13 (2): 102-7.
Ambler, R. P. Scott. Partial aminoacid sequence of penicillinase coded by Escherichia coli plasmid R6K. Proc. Acad. Sci. USA 1978; 75 (8): 3732-3736.
Bush, K., Jacob, G. A., Medeiros, A. A. A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob Agents Chemother. 1995; 39 (6): 1211-1233.
Metuor Dabiré A., Zongo KJ, Zeba B., Moussawi J., Baucher M. and El Jaziri M. Resistances to the oxyimino-cephalosporins by ctx-m-15 producing Klebsiella isolated from the urine samples of patients the university hospital complex pediatric charles de gaulle (chup-cdg) of ouagadougou in Burkina faso. Journal of Asian Scientific Research, 2013; 3 (9): 882-890.
Metuor Dabiré A., Zongo KJ, Zeba B., Traoré / Ouedraogo R., Moussawi J., Baucher M. and El Jaziri M. First detection of shv-type extended spectrum β-lactamases in the university hospital complex paediatric Charles de Gaulle (chup-cdg) of Ouagadougou in Burkina faso. Journal of Asian Scientific Research, 2014; 4 (5): 214-221.
Pagani L, Dell’Amico E, Migliavacca R., 2003. Multiple CTX-M-type extended spectrum beta-lactamases in nosocomial isolates of Enterobacteriaceae from a hospital in northern Italy. J Clin Microbiol; 41: 4264-9.
Sanders, C. C. β-lactamases of Gram-negative bacteria: New challenges for new drugs. Clin. Infect. Dis. 1992; 14: 1098-1099.
Jacoby, G. A. The genetics of extended-spectrum beta-lactamases. Eur. J. Clin. Microbiol. Infect. Dis. 1994; 13 (1): 2-11.
GangouéPiéboji J. Resistance of gram-negative bacilli to antibiotics: prevalence and characterization of broad-spectrum β-lactamases at Yaounde Central Hospital. PhD Thesis, University of Yaoundé I, 2000; 210 p.
Poiret, L., Naas, T., Thomas, I., Karim, A., Bingen, E., & P. Nordman. CTX-M-type extended-spectrum β-lactamasethat hydrolyses ceftazidime through a single aminoacid substitution in the Omega loop. Antimicrob. Agents Chemother. 2001; 45 (12): 3355-3361.
Bonnet R., Growing group of extended-spectrum β-lactamases: the CTX-M enzymes. Antimicrob Agents Chemother; 2004; 48 (12): 1-14.
Iabadene H, Messai Y, Ammari H, et al. Dissemination of ESBL and Qnr determinants in Enterobacter cloacae in Algeria. J AntimicrobChemother 2008; 62 (6): 133-6.
Bonnet R. Growing group of extended-spectrum _-lactamases: the CTX-M enzymes. Antimicrob Agents Chemother 2004; 48 (2): 1-14.
Zeba, B., Simporé, J., Nacoulma O G., Brother, J. M. Identification of metallo-β-lactamases from a clinicalisolate at St. Camille Medical Center of Ouagadougou / Burkina Faso. African Journal of Biotechnology 2005 4 (3): 286-288.