Lactoferrin Structure and Functions

  • Dominique Legrand
  • Annick Pierce
  • Elisabeth Elass
  • Mathieu Carpentier
  • Christophe Mariller
  • Joël Mazurier
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 606)


Lactoferrin (Lf) is an iron binding glycoprotein of the transferrin family that is expressed in most biological fluids and is a major component of mammals’ innate immune system. Its protective effect ranges from direct antimicrobial activities against a large panel of microorganisms, including bacteria, viruses, fungi, and parasites, to anti-inflammatory and anticancer activities. This plethora of activities is made possible by mechanisms of action implementing not only the capacity of Lf to bind iron but also interactions of Lf with molecular and cellular components of both host and pathogens. This chapter summarizes our current understanding of the Lf structure-function relationships that explain the roles of Lf in host defense.


Herpes Simplex Virus Type Human Lactoferrin Bovine Lactoferrin Biophysical Research Communication Fecal Lactoferrin 
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© Springer Science+Business Media, LLC 2008

Authors and Affiliations

  • Dominique Legrand
    • 1
  • Annick Pierce
  • Elisabeth Elass
  • Mathieu Carpentier
  • Christophe Mariller
  • Joël Mazurier
  1. 1.Unité de Glycobiologie Structurale et Fontionnelle, UMR n°8576 du CNRS, IFR 147 Université des Sciences et des Technologies de LilleF-59655 Villeneuve d’Ascq CedexFrance

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