Isolation of bacterial strains from bovine fecal microflora capable of degradation of ceftiofur

Veterinary Microbiology

Volumn 139, Issue 1-2, 2009, Pages 89-96

  Rafii, Fatemeh ^a   Williams, Anna J ^a   Park, Miseon ^a   Sims, Lillie M ^a   Heinze, Thomas M ^a   Cerniglia, Carl E ^a   Sutherland, John B ^a  

^a NATIONAL CENTER FOR TOXICOLOGICAL RESEARCH   (United States)

Author keywords

Beta lactamases; Biodegradation; Ceftiofur; Cephalosporins

Indexed keywords

AMPICILLIN; AZTREONAM; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CARBENICILLIN; CEFALOTIN; CEFOTAXIME; CEFOXITIN; CEFTAZIDIME; CEFTIOFUR; CLAVULANIC ACID; CLOXACILLIN; IMIPENEM; NITROCEFIN; OXACILLIN; PENICILLIN G;

ANALYTIC METHOD; ANTIBIOTIC SENSITIVITY; ARTICLE; AZOSPIRILLUM; BACILLUS; BACTERIAL GROWTH; BACTERIAL STRAIN; BACTERICIDAL ACTIVITY; BACTERIUM ISOLATION; CENTRIFUGATION; CONTROLLED STUDY; COW; CULTURE MEDIUM; DRUG DEGRADATION; DRUG METABOLISM; DRUG TRANSFORMATION; ENTEROCOCCUS CASSELIFLAVUS; ENZYME ACTIVITY; ENZYME SYNTHESIS; FECES MICROFLORA; GROWTH INHIBITION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; INCUBATION TIME; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; NUCLEOTIDE SEQUENCE; SUPERNATANT;

ANIMALS; ANTI-BACTERIAL AGENTS; AZOSPIRILLUM; BACILLUS; BETA-LACTAMASES; CATTLE; CEPHALOSPORINS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DRUG RESISTANCE, BACTERIAL; DRUG RESISTANCE, MULTIPLE, BACTERIAL; ENTEROCOCCUS; FECES; GENES, RRNA; METHYLOBACTERIACEAE; MICROBIAL SENSITIVITY TESTS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

ANIMALIA; AZOSPIRILLUM SP.; BACILLUS (BACTERIUM); BACILLUS PUMILUS; BACTERIA (MICROORGANISMS); BOVINAE; KOCURIA RHIZOPHILA; ROSEOMONAS;

EID: 70349246692     PISSN: 03781135     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vetmic.2009.04.023     Document Type: Article

References (35)

1. Beconi-Barker, M.G., Roof, R.D., Vidmar, T.J., Hornish, R.E., Smith, E.B., Gatchell, C.L., Gilbertson, T.J., 1996. Ceftiofur sodium: absorption, distribution, metabolism, and excretion in target animals and its determination by high-performance liquid chromatography. In: Moats, W.A., Medina, M.B. (Eds.), Veterinary Drug Residues: Food Safety, Amer. Chem. Soc. Symp. Ser. 636, pp. 70-84.
2. Boggio S.B., and Roveri O.A. Catalytic properties of an endogenous β-lactamase responsible for the resistance of Azospirillum lipoferum to β-lactam antibiotics. Microbiology 149 (2003) 445-450
3. Bush K. New β-lactamases in Gram-negative bacteria: diversity and impact on the selection of antimicrobial therapy. Clin. Infect. Dis. 32 (2001) 1085-1089
4. Bush K., Jacoby G.A., and Medeiros A.A. A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39 (1995) 1211-1233
5. Cid H., Carrillo O., Bunster M., Martínez J., and Vargas V. The relationship between the structures of four β-lactamases obtained from Bacillus cereus. Arch. Biol. Med. Exp. (Santiago) 21 (1988) 101-107
6. Clinical Laboratory Standards Institute. Performance Standards for Antimicrobial Disk Susceptibility Tests; Approved Standard M2-A9. 9th ed. (2006), CLSI, Wayne, Pennsylvania
7. Collatz E., Labia R., and Gutmann L. Molecular evolution of ubiquitous β-lactamases towards extended-spectrum enzymes active against newer β-lactam antibiotics. Mol. Microbiol. 4 (1990) 1615-1620
8. Elander R.P. Industrial production of β-lactam antibiotics. Appl. Microbiol. Biotechnol. 61 (2003) 385-392
9. Gilbertson T.J., Hornish R.E., Jaglan P.S., Koshy K.T., Nappier J.L., Stahl G.L., Cazers A.R., Nappier J.M., Kubicek M.F., Hoffman G.A., and Hamlow P.H. Environmental fate of ceftiofur sodium, a cephalosporin antibiotic. Role of animal excreta in its decomposition. J. Agric. Food Chem. 38 (1990) 890-894
10. Gilbertson T.J., Roof R.D., Nappier J.L., Zaya M.J., Robins R.H., Stuart D.J., Krzeminski L.F., and Jaglan P.S. Disposition of ceftiofur sodium in swine following intramuscular treatment. J. Agric. Food Chem. 43 (1995) 229-234
11. Hall B.G., and Barlow M. Evolution of the serine β-lactamases: past, present and future. Drug Resist. Updat. 7 (2004) 111-123
12. Henderson T.A., Young K.D., Denome S.A., and Elf P.K. AmpC and AmpH, proteins related to the class C β-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli. J. Bacteriol. 179 (1997) 6112-6121
13. Hornish R.E., and Kotarski S.F. Cephalosporins in veterinary medicine-ceftiofur use in food animals. Curr. Top. Med. Chem. 2 (2002) 717-731
14. Jacoby G.A., and Munoz-Price L.S. The new β-lactamases. N. Engl. J. Med. 352 (2005) 380-391
15. Jaglan P.S., Kubicek M.F., Arnold T.S., Cox B.L., Robins R.H., Johnson D.B., and Gilbertson T.J. Metabolism of ceftiofur. Nature of urinary and plasma metabolites in rats and cattle. J. Agric. Food Chem. 37 (1989) 1112-1118
16. Janda J.M., and Abbott S.L. 16S rRNA gene sequencing for bacterial identification in the diagnostic laboratory: pluses, perils, and pitfalls. J. Clin. Microbiol. 45 (2007) 2761-2764
17. Kobayashi T., Zhu Y.F., Nicholls N.J., and Lampen J.O. A second regulatory gene, blaR1, encoding a potential penicillin-binding protein required for induction of β-lactamase in Bacillus licheniformis. J. Bacteriol. 169 (1987) 3873-3878
18. Koshy K.T., and Cazers A.R. Controlled hydrolysis of ceftiofur sodium, a broad-spectrum cephalosporin; isolation and identification of hydrolysis products. J. Pharm. Sci. 86 (1997) 389-395
19. Lee E.-W., Huda M.N., Kuroda T., Mizushima, and Tsuchiya T. EfrAB, an ABC multidrug efflux pump in Enterococcus faecalis. Antimicrob. Agents Chemother. 47 (2003) 3733-3738
20. Li X.-Z., Mehrotra M., Ghimire S., and Adewoye L. β-Lactam resistance and β-lactamases in bacteria of animal origin. Vet. Microbiol. 121 (2007) 197-214
21. Liras P., and Martín J.F. Gene clusters for β-lactam antibiotics and control of their expression: why have clusters evolved, and from where did they originate?. Int. Microbiol. 9 (2006) 9-19
22. Livermore D.M., and Brown D.F.J. Detection of β-lactamase-mediated resistance. J. Antimicrob. Chemother. 48 Suppl. S1 (2001) 59-64
23. Livermore D.M., and Williams J.D. β-Lactams: mode of action and mechanisms of bacterial resistance. In: Lorian V. (Ed). Antibiotics in Laboratory Medicine. 4th ed. (1996), Williams & Wilkins, Baltimore, MD 502-578
24. Murray B.E., and Mederski-Samaroj B. Transferable β-lactamase: a new mechanism for in vitro penicillin resistance in Streptococcus faecalis. J. Clin. Invest. 72 (1983) 1168-1171
25. Popelka P., Nagy J., Germuška R., Marcinčák S., Jevinová P., and de Rijk A. Comparison of various assays used for detection of beta-lactam antibiotics in poultry meat. Food Addit. Contam. 22 (2005) 557-562
26. Rafii F. Beta-lactam resistance in enterococci. In: Kobayashi N. (Ed). Drug Resistance of Enterococci: Epidemiology and Molecular Mechanisms (2006), Research Signpost, Trivandrum, Kerala, India 101-115
27. Rihs J.D., Brenner D.J., Weaver R.E., Steigerwalt A.G., Hollis D.G., and Yu V.L. Roseomonas, a new genus asociated with bacteremia and other human infections. J. Clin. Microbiol. 31 (1993) 3275-3283
28. Salmon S.A., Watts J.L., and Yancey Jr. R.J. In vitro activity of ceftiofur and its primary metabolite, desfuroylceftiofur, against organisms of veterinary importance. J. Vet. Diagn. Invest. 8 (1996) 332-336
29. Sarmah A.K., Meyer M.T., and Boxall A.B.A. A global perspective on the use, sales, exposure pathways, occurrence, fate and effects of veterinary antibiotics (VAs) in the environment. Chemosphere 65 (2006) 725-759
30. Sunkara G., Navarre C.B., and Kompella U.B. Influence of pH and temperature on kinetics of ceftiofur degradation in aqueous solutions. J. Pharm. Pharmacol. 51 (1999) 249-255
31. Turner P.J. Extended-spectrum β-lactamases. Clin. Infect. Dis. 41 Suppl. 4 (2005) S273-S275
32. Vercauteren E., Descheemaeker P., Ieven M., Sanders C.C., and Goossens H. Comparison of screening methods for detection of extended-spectrum β-lactamases and their prevalence among blood isolates of Escherichia coli and Klebsiella spp. in a Belgian teaching hospital. J. Clin. Microbiol. 35 (1997) 2191-2197
33. Walsh C. Antibiotics: Actions, Origins, Resistance (2003), ASM Press, Washington, DC p. 345
34. Weisburg W.G., Barns S.M., Pelletier D.A., and Lane D.J. 16S ribosomal DNA amplification for phylogenetic study. J. Bacteriol. 173 (1991) 697-703
35. Zapun A., Contreras-Martel C., and Vernet T. Penicillin-binding proteins and β-lactam resistance. FEMS Microbiol. Rev. 32 (2008) 361-385