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Cofactor Requirements for Expression of Lactoferrin Bactericidal Activity on Enteric Bacteria

  • M. A. Motley
  • R. R. Arnold
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 216 A)

Abstract

Lactoferrin (LF), is an iron-binding glycoprotein that is common to most mammalian excretions (1–3) and is a prominent component of the specific granule of neutrophilic leukocytes (4,5). It shares its distribution on mucosal surfaces with that of secretory IgA. Its high affinity binding in coordination with suitable anion has been well characterized (6–9). This ability to bind iron has been associated with a bacteriostatic deprivation of this essential nutrient (10–12). A variety of other biological activities have also been attributed to LF, including a direct bactericidal effect on a variety of bacteria (13,14). This killing mechanism is temperature and pH dependent and requires direct interaction of the LF with the bacterial cell surface (15). There are a variety of bacteria that are resistant to the bactericidal effects of purified LF binding including selected Gramnegative enteric bacteria (14). The resistance of these bacteria appears related, in part, to the impermeability of their outer cellular structures (16).

Keywords

Bactericidal Activity Void Volume Enteric Bacterium Bacteriostatic Activity Human Colostrum 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • M. A. Motley
    • 1
  • R. R. Arnold
    • 2
  1. 1.Department of Microbiology and ImmunologyMorehouse School of MedicineAtlantaUSA
  2. 2.Department of Oral BiologyEmory University Dental Research CenterAtlantaUSA

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