DOI QR코드

DOI QR Code

A novel method to depurate β-lactam antibiotic residues by administration of a broad-spectrum β-lactamase enzyme in fish tissues

  • Choe, Young-Sik (Department of Aquatic Life Medicine, College of Ocean Sciences, Kunsan National University) ;
  • Lee, Ji-Hoon (Department of Aquatic Life Medicine, College of Ocean Sciences, Kunsan National University) ;
  • Jo, Soo-Geun (Department of Aquatic Life Medicine, College of Ocean Sciences, Kunsan National University) ;
  • Park, Kwan Ha (Department of Aquatic Life Medicine, College of Ocean Sciences, Kunsan National University)
  • Received : 2016.01.06
  • Accepted : 2016.12.02
  • Published : 2016.12.31

Abstract

As a novel strategy to remove ${\beta}$-lactam antibiotic residues from fish tissues, utilization of ${\beta}$-lactamase, enzyme that normally degrades ${\beta}$-lactam structure-containing drugs, was explored. The enzyme (TEM-52) selectively degraded ${\beta}$-lactam antibiotics but was completely inactive against tetracycline-, quinolone-, macrolide-, or aminoglycoside-structured antibacterials. After simultaneous administration of the enzyme with cefazolin (a ${\beta}$-lactam antibiotic) to the carp, significantly lowered tissue cefazolin levels were observed. It was confirmed that the enzyme successfully reached the general circulation after intraperitoneal administration, as the carp serum obtained after enzyme injection could also degrade cefazolin ex vivo. These results suggest that antibiotics-degrading enzymes can be good candidates for antibiotic residue depuration.

Keywords

References

  1. Abraham EP, Chain E. An enzyme from bacteria is able to destroy penicillin. 1940. Rev Infect Dis. 1988;10:677-8. https://doi.org/10.1093/clinids/10.4.677
  2. Bush K, Jacoby GA, Medeiros AA. A functional classification scheme for ${\beta}$-lactamases and its correlation with molecular structure. Antimicrob Agents Chemother. 1995;39:1211-33. https://doi.org/10.1128/AAC.39.6.1211
  3. Cabello FC. Heavy use of prophylactic antibiotics in aquaculture: a growing problem for human and animal health and for the environment. Environ Microbiol. 2006;8:1137-44. https://doi.org/10.1111/j.1462-2920.2006.01054.x
  4. De Pascale G, Wright GD. Antibiotic resistance by enzyme inactivation: from mechanisms to solutions. Chem Biol Chem. 2010;11:1326-34.
  5. Flessner MF. The transport barrier in intraperitoneal therapy. Am J Ren Physiol. 2005;288:F433-42. https://doi.org/10.1152/ajprenal.00313.2004
  6. Hong S, Secombe CJ. Two peptides derived from trout IL-$1{\beta}$ have different stimulatory effects on immune gene expression after intraperitoneal administration. Comp Biochem Physiol Part B. 2009;153:275-80. https://doi.org/10.1016/j.cbpb.2009.03.008
  7. Livermore DM. ${\beta}$-lactamases in laboratory and clinical resistance. Clin Microbiol Rev. 1995;8:557-84.
  8. Matagne A, Dubus A, Galleni M, Frere JM. The beta-lactamase cycle: a tale of selective pressure and bacterial ingenuity. Nat Prod Rep. 1999;16:1-19. https://doi.org/10.1039/a705983c
  9. Murashita K, Jordal AO, Nilsen TO, Stefansson SO, Kurokawa T, Bjornsson BT, Moen AG, Ronnestad I. Leptin reduces Atlantic salmon growth through the entral pro-opiomelanocortin pathway. Comp Biochem Physiol Part A. 2010;158:79-86.
  10. Nadai M, Hasegawa T, Kato K, Wang L, Nabeshima T, Kato N. Antimicrob Agents Chemother. 1993;37:1781-5. https://doi.org/10.1128/AAC.37.9.1781
  11. O'Callaghan CH, Morris A, Kirby SM, Shingler AH. Novel method for detection of beta-lactamases by using a chromogenic cephalosporin substrate. Antimicrob Agents Chemother. 1972;4:283-8.
  12. Pai H, Lyu S, Lee JH, Kim J, Kwon Y, Kim JW, Choe KW. Survey of extendedspectrum ${\beta}$-lactamases in clinical isolates of Escheria coli and Klebsiella pneumoniae: prevalence of TEM-52 in Korea. J Clin Microbiol. 1999;37:1758-63.
  13. Perilli M, Segatore B, De Massis MR, Pagani L, Luzzaro F, Rossolini GM, Amicosante G. Biochemical characterization of TEM-92 extendedspectrum b-lactamase, a protein differing from TEM-52 in the signal peptide. Antimicrob Agent Chemother. 2002;46:3981-3. https://doi.org/10.1128/AAC.46.12.3981-3983.2002
  14. Poyart C, Mugnier P, Quesne G, Berche P, Trieu-Cuot P. A novel extendedspectrum TEM-type ${\beta}$-lactamse (TEM-52) associated with decreased susceptibility to moxalactam in Klebsiella pneumoniae. Antimicrob Agents Chemother. 1998;42:108-13.
  15. Shahada F, Chuma T, Dahshan H, Akiba M, Sueyoshi M, Okamoto K. Detection and characterization of extend-spectrum ${\beta}$-latamase (TEM-52)-producing Salmonella serotype infantis from broilers in Japan. Foodborne Pathogens Dis. 2010;7:515-21. https://doi.org/10.1089/fpd.2009.0454