Influence of zinc, sodium bicarbonate, and citric acid on the antibacterial activity of ovotransferrin against Escherichia coli O157:H7 and Listeria monocytogenes in model systems and ham

Poultry Science

Volumn 87, Issue 12, 2008, Pages 2660-2670

  Ko, K Y ^a   Mendonca, A F ^a   Ahn, D U ^a  

^a NONE

Author keywords

Antibacterial activity; Bicarbonate; Citric acid; Escherichia coli O157:H7; Ovotransferrin

Indexed keywords

ESCHERICHIA COLI; LISTERIA MONOCYTOGENES;

EID: 57049118092     PISSN: 00325791     EISSN: 15253171     Source Type: Journal    
DOI: 10.3382/ps.2007-00503     Document Type: Article

References (59)

1. Abdallah, F. B., and J. M. Chahine. 1999. Transferrins, the mechanism of iron release by ovotransferrin. Eur. J. Biochem. 263:912-920.
2. Abdallah, F. B., and J. M. el Hage Chahine. 1998. Hen ovo-transferrin, interaction with bicarbonate and iron uptake. Eur. J. Biochem. 258:1022-1031.
3. Abola, J. E., M. C. Wood, A. Chwen, D. Abraham, and P. D. Pulsinelli. 1982. Pages 27-34 in The Biochemistry and Physiology of Iron. P. Saltman and J. Hegenauer, ed. Elsevier Biomedical Inc., Amsterdam, the Netherlands.
4. Aguilera, O., M. Luis, L. M. Quirosb, and J. F. Fierro. 2003. Transferrins selectively cause ion efflux through bacterial and artificial membranes. FEBS Lett. 548:5-10.
5. Aisen, P. 1989. Physical biochemistry of the transferrins - Uptake. Pages 353-371 in Iron Carriers and Ion Proteins. T. Loehr, ed. VCH, New York, NY.
6. Aisen, P., and I. Listowsky. 1980. Iron transport and storage proteins. Annu. Rev. Biochem. 49:357-393.
7. Amézquita, A., and M. M. Brashears. 2002. Competitive inhibition of Listeria monocytogenes in ready-to-eat meat products by lactic acid bacteria. J. Food Prot. 65:316-325.
8. Anderson, B. F., H. M. Baker, G. E. Norris, D. W. Rice, and E. N. Baker. 1989. Structure of human lactoferrin-crystallographic structure analysis and refinement at 2.8 Å resolution . J. Mol. Biol. 209:711-734.
9. Appelmelk, B. J., Y. Q. An, M. Geerts, B. G. Thijs, H. A. de Boer, D. M. MacLaren, J. de Graaff, and J. H. Nuijens. 1994. Lactoferrin is a lipid A-binding protein. Infect. Immun. 62:2628-2632.
10. Arnold, R. R., M. Brewer, and J. J. Gauthier. 1980. Bactericidal activity of human lactoferrin: Sensitivity of a variety of microorganisms. Infect. Immun. 28:893-898.
11. Arnold, R. R., J. E. Russel, W. J. Chempion, and J. J. Gauthier. 1981. Bactericidal activity of human lactoferrin: Influence of physical conditions and metabolic state of the target microorganism. Infect. Immun. 32:655-660.
12. Bailey, C. T., M. G. Patch, and C. J. Carrion. 1988. Affinity labels for the anion-binding site in ovotransferrin. Biochemistry 27:6276-6282.
13. Baron, F., S. Fauve, and M. Gautier. 2000. Pages 417-440 in Egg Nutrition and Biotechnology. J. S. Sim, S. Nakai, and W. Günter, ed. CAB Int., Oxfordshire, UK.
14. Baron, F., M. Gautier, and G. Brule. 1997. Factors involved in the inhibition of Salmonella Enteritidis in liquid egg white. J. Food Prot. 60:1318-1323.
15. Baveye, S., E. Leas, J. Maurer, G. Spike, and D. Lybrand. 1999. Lactoferrin: A multi-functional glycoprotein involved in the modulation of the inflammatory process. Clin. Chem. Lab. Med. 37:281-286.
16. Bellounis, L., R. Acadian, and J. M. El Hage Chahine. 1996. Apo-transferrin proton dissociation and interactions with bicarbonate in neutral media. J. Phys. Org. Chem. 9:111-118.
17. Bishop, J. G., F. L. Schumacher, L. C. Ferguson, and K. L. Smith. 1976. In vitro growth inhibition of mastitis-causing coliform bacteria by bovine apo-lactoferrin and reversal of inhibition by citrate and high concentrations of apo-lactoferrin. Infect. Immun. 14:911-918.
18. Brock, J. H. 1985. The transferrins. Pages 183-262 in Metalloproteinase II. P. Harrison, ed. MacMillan Press, London, UK.
19. Brock, J. H. 2002. The physiology of lactoferrin. Biochem. Cell Biol. 80:1-6.
20. Butterworth, R. M., J. F. Gibson, and J. Williams. 1975. Electron-paramagnetic-resonance spectroscopy of iron-binding fragments of hen ovotransferrins. Biochem. J. 149:559-563.
21. Corral, L. G., L. S. Post, and T. J. Montville. 1988. Antimicrobial activity of sodium bicarbonate. J. Food Sci. 53:981-982.
22. Czuprynski, C. J., and N. G. Faith. 2002. Sodium bicarbonate enhances the severity of infection in neutropenic mice orally inoculated with Listeria monocytogenes EGD. Clin. Diagn. Lab. Immunol. 9:477-481.
23. Eaton, S. S., J. Dubach, G. R. Eaton, G. Thurman, and D. R. Ambruso. 1990. Electron spin echo envelope modulation evidence for carbonate binding to iron(III) and copper(II) transferrin and lactoferrin. J. Biol. Chem. 265:7138-7141.
24. Elass-Rochard, E., A. Roseanu, D. Legrand, M. Trif, V. Salmon, C. Motas, J. Montreuil, and G. Spik. 1995. Lactoferrin-lipopolysaccharides interaction: Involvement of the 28-34 loop region of human lactoferrin in the high-affinity binding to Escherichia coli 055B5 lipopolysaccharides. Biochem. J. 312:839-845.
25. Ellison, R. T. III, and T. J. Giehl. 1991. Killing of gram-negative bacteria by lactoferrin and lysozyme. J. Clin. Invest. 88:1080-1091.
26. Ellison, R. T. III, T. J. Giehl, and F. M. Laforce. 1988. Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin. Infect. Immun. 56:2774-2781.
27. Fraenkel-Conrat, H., and R. E. Feeney. 1950. The metal-binding activity of conalbumin. Arch. Biochem. 29:101-113.
28. Frost, G. E., and H. Rosemberg. 1973. The citrate-dependent iron transport system in Escherichia coli K-12. Biochim. Biophys. Acta 330:90-101.
29. Griffiths, E., and J. Humphreys. 1977. Bacteriostatic effect of human milk and bovine colostrum on Escherichia coli. Importance of bicarbonate . Infect. Immunol. 15:396-401.
30. Ibrahim, H. R. 1997. Insights into the structure-function relationship of ovalbumin, ovotransferrin and lysozyme. Pages 37-56 in Hen Eggs: Their Basic and Applied Science. T. Yamamoto, I. R. Juneja, H. Hatta, and M. Kim, ed. CRC Press, Boca Raton, FL.
31. Ibrahim, H. R., Y. Sugimoto, and T. Aoki. 2000. Ovotransferrin antimicrobial peptide (OATP-92) kills bacteria through a membrane damage mechanism. Biochim. Biophys. Acta 1523:196-205.
32. Kuehl, R. O. 2000. Design of Experiments: Statistical Principles of Research Design and Analysis. 2nd ed. Duxbury Press, New York, NY.
33. Kurokawa, H., J. C. Dewan, B. Mikami, and J. C. Sacchettini. 1999. Crystal structure of apo-hen ovotransferrin. J. Biol. Chem. 274:28445-28452.
34. Lee, Y. L., T. Cesario, J. Owens, E. Shanbrom, and L. D. Thrupp. 2002. Antibacterial activity of citrate and acetate. Nutrition 18:665-666.
35. Lee, Y. L., L. Trupp, J. Owens, T. Cesario, and E. Shanbrom. 2001. Bactericidal activity of citrate against gram-positive cocci. Lett. Appl. Microbiol. 33:349-351.
36. Mann, D. M., E. Romm, and M. Migliorini. 1994. Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin. J. Biol. Chem. 269:23661-23667.
37. Naidu, A. S. 2002. Viable lactoferrin - A new approach to meat safety. Food Technol. 56:40-45.
38. Pakdaman, R., and J. M. El Hage Chahine. 1996. A mechanism for iron uptake by transferrin. Eur. J. Biochem. 236:922-931.
39. Pakdaman, R., and J. M. El Hage Chahine. 1997. Transferrin - The interaction of lactoferrin with hydrogen carbonate. Eur. J. Biochem. 249:149-155.
40. Pakdaman, R., M. Petitjean, and J. M. El Hage Chahine. 1998. Transferrins - A mechanism for iron uptake by lactoferrin. Eur. J. Biochem. 254:144-153.
41. Peaker, M., and J. L. Linzell. 1975. Citrate in milk: A harbinger of lactogenesis. Nature 253:464.
42. Phelps, C. F., and E. Antonini. 1975. A study of kinetics of iron and copper binding to hen ovotransferrin. Biochem. J. 147:385-391.
43. Rawas, A., H. Muirhead, and J. Williams. 1996. Structure of diferric duct ovo-transferrin at 2.35 Å resolution . Acta Crystallogr. D2:631-640.
44. Reiter, B., J. H. Brock, and E. D. Steel. 1975. Inhibition of Escherichia coli by bovine colostrum and post colostral milk. II. The bacteriostatic effect of lactoferrin on a serum susceptible and serum resistant strain of E. coli. Immunology 28:83-95.
45. 3+ by transferrin. J. Biol. Chem. 250:2182-2188.
46. Shimazaki, K. 2000. Lactoferrin: A marvelous protein in milk. Anim. Sci. J. 71:329-347.
47. Suzuki, Y. A., K. Shin, and B. Lonnerdal. 2002. Characterization of mammalian receptors for lactoferrin. Biochem. Cell Biol. 80:75-80.
48. Valenti, P., G. Antonin, C. Von Hunolstein, P. Visca, N. Orsi, and E. Antonini. 1983. Studies of the antimicrobial activity of ovotransferrin. Int. J. Tissue React. 1:97-105.
49. Valenti, P., G. Antonini, M. R. R. Fanelli, N. Orsi, and E. Antonini. 1982. Antibacterial activity of matrix-bound ovotransferrin. Antimicrob. Agents Chemother. 21:840-841.
50. Valenti, P., A. De Stasio, P. Mastromarino, L. Seganti, L. Sinibaldi, and N. Orsi. 1981. Influence of bicarbonate and citrate on the bacteriostatic action of ovotransferrin towards Staphylococci. FEMS Microbiol. Lett. 10:77-79.
51. 3 as a character of potential pathogenecity. J. Clin. Microbiol. 11:445-447.
52. Valenti, P., P. Visca, G. Antonini, and N. Orsi. 1985. Antifungal activity ovotransferrin towards genus Candida. Mycophathologia 89:169-175.
53. +2 and other metal ions on the antibacterial activity of ovotransferrin. Med. Microbiol. Immunol. (Berl.) 176:123-130.
54. Ward, P. P., S. Uribe-Luna, and O. M. Conneely. 2002. Lactoferrin and host defense. Biochem. Cell Biol. 80:95-102.
55. Warner, R. C., and I. Weber. 1953. The metal combining properties of conalbumin. J. Am. Chem. Soc. 75:5094-5101.
56. Williams, J., R. W. Evans, and K. Moreton. 1978. The iron-binding properties of hen ovotransferrin. Biochem. J. 173:535-542.
57. Woodworth, R. C., L. M. Virkaitis, R. G. Woodbury, and R. A. Fava. 1975. Pages pp 39-50 in Proteins of Ion Storage and Transport in Biochemistry and Medicine. R. R. Crichton, ed. North-Holland, Amsterdam, the Netherlands.
58. Zhu, M. J., A. Mendonca, H. A. Ismail, and D. U. Ahn. 2004. Effects of irradiation on survival and growth of Listeria monocytogenes and natural microflora in vacuum packaged turkey hams and breast rolls. PhD Thesis. Iowa State University, Ames.
59. Zuccola, H. J. 1992. The crystal structure of monoferric human serum transferrin. PhD Thesis. University of Michigan, Ann Arbor.