Skip to main content

Antimicrobial Properties of Iron-Binding Proteins

  • Chapter
Diet and Resistance to Disease

Abstract

Iron-binding proteins of the transferrin type occur widely in various biological fluids. Serum transferrins (serotransferrins) are necessary to transport iron into the immature red cells of the bone marrow for hemoglobin synthesis, and to accept iron from the reticuloendothelial system as the latter destroys senescent or damaged red cells and releases iron from hemoglobin. The discovery of the transferrins is, however, closely related to another property thereof, i.e., the inhibition of bacterial growth. Thus, in 1944, Schade and Caroline discovered that raw egg-white was bacteriostatic and that this activity could be abolished by the addition of iron to the egg-white (Schade and Caroline, 1944). Two years later it was shown that the antimicrobial substance present in the egg-whites was a transferrin-type protein called conalbumin (Alderton et al., 1946), which had been discovered half-a-century earlier by Osborne and Campbell (1900), who were totally unaware of either the antimicrobial or the iron-binding properties of the protein. Schade and Caroline (1946) also described the antimicrobial properties of serotransferrin, which could also be abolished by the addition of iron. It is today recognized that serotransferrin has a function in host-defense mechanisms in addition to its function as a mediator of iron-cell interactions.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

eBook
USD 16.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 16.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Aisen, P., and Leibman, A. (1972) Lactoferrin and transferrin: a comparative study. Biochim. Biophys. Acta 257: 314–323.

    CAS  Google Scholar 

  • Aisen, P., and Brown, E. B. (1975) Structure and function of transferrins, Prog. in Hematol. 9: 25–56.

    CAS  Google Scholar 

  • Aisen, P., Leibman, A., and Zweier, J. (1978) Stoichiometric and site characteristics of the binding of iron to human transferrin. J. Biol. Chem. 253: 1930–1937.

    CAS  Google Scholar 

  • Alderton, G., Ward, W. H., and Fevold, H. L. (1946) Identification of the bacteria-inhibiting iron-binding protein of egg-white as conalbumin, Arch. Biochem Biophys. 11: 9–13.

    CAS  Google Scholar 

  • Arnold, R. R., Cole, M. F., and McGhee, J. R. (1977) A bactericidal effect of human lactoferrin. Science 197: 263–265.

    Article  CAS  Google Scholar 

  • Barry, D. M. J., and Reeve, A. W. (1977) Increased incidence of gram-negative neonatal sepsis with intramuscular Iron administration. Pediatrics 60: 908–912.

    CAS  Google Scholar 

  • Becroft, D. M. O., Dix, M. R., and Farmer, K. (1977) Intramuscular iron-dextran and susceptibility of neonates to bacterial infections. Arch. Dis. in Childh. 52: 778–781.

    Article  CAS  Google Scholar 

  • Bezkorovainy, A (1977) Human milk and colostrum proteins: a review. J. Dairy Sci. 60: 1023–1037.

    Article  CAS  Google Scholar 

  • Bezkorovainy, A. (1980) “Non-Heme Iron Biochemistry”. Plenum Press, New York, in press.

    Google Scholar 

  • Bezkorovainy, A., and Zschocke, R. H. (1974) Structure and function of transferrins. I. Physical, chemical, and iron-binding properties, Arzneimittel-Forschung 24: 476–485.

    CAS  Google Scholar 

  • Bullen, J. J., and Armstrong, J. A. (1979) The role of lactoferrin in the bactericidal function of polymorphonuclear leucocytes. Immunology 36: 781–791.

    CAS  Google Scholar 

  • Bullen, J. J., Rogers, H. J., and Leigh, L. (1972) Iron-binding proteins in milk and resistance to Escherichia coli infection in infants. Brit, Med. J. 1: 69–75.

    Article  CAS  Google Scholar 

  • Bullen, J. J., Rogers, H. J., and Griffiths, E. (1978) Role of iron in bacterial infection. Curr. Topics in Microbiol. 80: 1–35.

    Article  CAS  Google Scholar 

  • Calver, G. A., Kenny, C. P., and Kushner, D. J. (1979) Inhibition of the growth of Neisseria meningitidis by reduced ferritin and other iron-binding agents. Infection and Immunity 25: 880–890.

    CAS  Google Scholar 

  • Caroline, L., Rosner, F., and Kozina, P. J. (1969) Elevated serum iron, low unbound transferrin, and candidiasis in acute leukemia. Blood 34: 441–451.

    CAS  Google Scholar 

  • Chasteen, D. (1977) Human serotransferrins: structure and function. Coord. Chem. Revs. 22: 1–36.

    Article  CAS  Google Scholar 

  • Cox, T. M., Mazurier, J., Spik, G., Montreuil, J., and Peters, T. (1979) Iron-binding proteins and influx of iron across the duodenal brush border: evidence for specific lactoferrin receptors in the human intestine. Biochim. Biophys. Acta 588: 120– 128.

    Article  CAS  Google Scholar 

  • Editorial (1975) The relationship between infection and the iron status of an individual, Nutr. Revs. 33: 103–105.

    Google Scholar 

  • Fletcher, J., and Huehns, E. R. (1968) Function of transferrin. Nature 218: 1211–1214.

    Article  CAS  Google Scholar 

  • Frieden, E., and Aisen, P. (1980) Forms of iron transferrin. Trends in Biochem. Sci. 5: XI.

    Article  CAS  Google Scholar 

  • Ganzoni, A. M., and Puschmann, M (1977) Iron status and host defense, in: Brown, E. B., Aisen, P., Fielding, J., and Crichton, R. R. (eds.), “Proteins of Iron Metabolism”, Grune and Stratton, Publ., New York, pp. 427–432.

    Google Scholar 

  • Goldman, A. S. (1973) Host resistance factors in human milk. J. Peds. 82: 1082–1090.

    Article  CAS  Google Scholar 

  • Gorinsky, B., Horsburgh, C., Lindley, P. F., Moss, D. S., Parkar, M., and Watson, J. L. (1979) Evidence for the bilobal nature of diferric rabbit plasma transferrin. Nature 281: 157–158.

    Article  CAS  Google Scholar 

  • Griffiths, E., and Humphreys, J. (1977) Bacteriostatic effect of human milk and bovine colostrum on Escherichia coli; the importance of bicarbonate. Infection and Immunity 15: 396–401.

    CAS  Google Scholar 

  • Grohlich, D., Morley, C. G. D., and Bezkorovainy, A. (1980) unpublished results.

    Google Scholar 

  • Harmon. R. J., Schanbacher, F. L., Ferguson, L. C., and Smith, K. L. (1976) Changes in lactoferrin, immunoglobulin G, bovine serum albumin, and α-lactalbumin during acute experimental and natural coliform mastitis in cows. Infection and Immunity 13: 533–542.

    CAS  Google Scholar 

  • Jones, R. L., Peterson, C. M., Grady, R. W., Kumbaraci, T., Cerami, A., and Graziano, J. H. (1977) Effects of iron chelators and iron overload on Salmonella infection. Nature 267: 63–64.

    Article  CAS  Google Scholar 

  • Kluger, M. J. and Rothenburg, B. A. (1979) Fever and reduced iron: their interaction as a host defense response to bacterial infection. Science 203: 374–376.

    Article  CAS  Google Scholar 

  • Kochan, I., Kvach, J. T., and Wiles, T. I. (1977) Virulence associated acquisition of iron in mammalian serum by Escherichia coli, J. Inf. Dis. 135: 623–632.

    Article  CAS  Google Scholar 

  • Kochan, I., Wasynczuk, J., and McCabe, M. (1978) Effects of injected iron and siderophores on infections in normal and immune mice. Infection and Immunity 22: 560–567.

    CAS  Google Scholar 

  • Kumar, R. (1979) Mechanism of anemia of chronic infection-estimation of labile iron pool and interpretation of ferrokinetic data. Ind. J. Med. Res. 70: 455–462.

    CAS  Google Scholar 

  • Kvach, J. T., Wiles, T. I., Mellencamp, M. W., and Kochan, I. (1977) Use of transferrin-iron-enterobactin complexes as the source of iron by serum-exposed bacteria. Infection and Immunity 18: 439–445.

    CAS  Google Scholar 

  • Law, B. A., and Reiter, B. (1977) The isolation and bacteriostatic properties of lactoferrin from bovine milk whey, J. Dairy Res. 44: 595–599.

    Article  CAS  Google Scholar 

  • Leibman, A., and Aisen, P. (1979) Distribution of iron between the binding sites of transferrin in serum: methods and results in normal human subjects. Blood 53:1058–1065.

    CAS  Google Scholar 

  • MacGillivray, R. T. A., Mendez, E., and Brew, K. (1977) Structure and evolution of serum transferrin, in: Brown, E. B., Aisen, P., Fielding, J., and Crichton, R. R. (eds.), “Proteins of Iron Metabolism”. Grune and Stratton, Publ., New York, pp. 133–141.

    Google Scholar 

  • McFarlane, H., Reddy, S., Adcock, K. J., Adeshina, H., Cooke, A. R., and Akene, J. (1970) Immunity, transferrin, and survival in kwashiorkor. Brit. Med. J. 4: 268–270.

    Article  Google Scholar 

  • Masson, P. L., Heremans, J. F., and Schonne, E. (1969) Lactoferrin, as iron-binding protein in neutrophilic leucocytes. J. Exptl. Med. 130: 643–658.

    Article  CAS  Google Scholar 

  • Miles, A. A., Khimji, P. L., and Maskell, J. (1979) The variable response of bacteria to excess ferric iron in host tissues. J. Med. Microbiol. 12: 17–28.

    Article  CAS  Google Scholar 

  • Neilands, J. B. (1974) “Microbial Iron Metabolism”. Academic Press, New York.

    Google Scholar 

  • Osborne, T. B., and Campbell, G. F. (1900) The protein constituents of egg white. J. Amer. Chem. Soc. 22: 422–450.

    Article  Google Scholar 

  • Payne, S. M., and Finkelstein, R. A. (1978) The critical role of iron in host-bacterial interactions. J. Clin. Inv. 61: 1428–1440.

    Article  CAS  Google Scholar 

  • Pearson, H. A., and Robinson, J. E. (1976) The role of iron in host resistance. Adv. in Pediatrics 23: 1–33.

    Article  CAS  Google Scholar 

  • Pollack, J. R., and Neilands, J. B, (1970) Enterobactin, an iron transport compound. Biochem. Biophys. Res. Comm. 38: 989–992.

    Article  CAS  Google Scholar 

  • Rogers, H. J., Bullen, J. J., and Cushnie, G. H. (1970) Iron compounds and resistance to infection. Further experiments with Clostridium welchii Type A in vivo and in vitro Immunology 19: 521–538.

    CAS  Google Scholar 

  • Schade, A. L., and Caroline, L. (1944) Raw hen egg white and the role of iron in growth inhibition of Shigella dysenteriae, Staphylococcus aureus, Escherichia coli, and Saccharomyces cerevisiae. Science 100: 14–15.

    Article  CAS  Google Scholar 

  • Schade, A. L., and Caroline, L. (1946) An iron-binding component in human blood plasma. Science 104: 340–341.

    Article  CAS  Google Scholar 

  • Shirashi, A., and Arai, T. (1979) Antifungal activity of transferrin. Sabouraudia 17: 79–83.

    Article  Google Scholar 

  • Torrance, J. D., Charlton, R. W., Simon, M. O., Lynch, S. R., and Bothwell, T. H. (1978) The mechanism of endotoxin-induced hypoferraemia. Scand. J. Haematol. 21: 403–410.

    Article  CAS  Google Scholar 

  • Weinberg, E. D. (1977) Infection and iron metabolism. Amer. J. Clin. Nutr. 30: 1485–1490.

    CAS  Google Scholar 

  • Weinberg, E. D. (1978) Iron and infection. Microbiol. Revs. 42: 45–66.

    CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1981 Plenum Press, New York

About this chapter

Cite this chapter

Bezkorovainy, A. (1981). Antimicrobial Properties of Iron-Binding Proteins. In: Phillips, M., Baetz, A. (eds) Diet and Resistance to Disease. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9200-6_8

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-9200-6_8

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4615-9202-0

  • Online ISBN: 978-1-4615-9200-6

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics