Legrand Dominique, Pierce Annick, Elass Elisabeth, Carpentier Mathieu, Mariller Christophe, Mazurier Joël
Unité de Glycobiologie Structurale et Fontionnelle, UMR 8576 du CNRS, IFR 147, Université des Sciences et des Technologies de Lille, F-59655 Villeneuve d'Ascq Cedex, France.
Adv Exp Med Biol. 2008;606:163-94. doi: 10.1007/978-0-387-74087-4_6.
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.
乳铁蛋白(Lf)是转铁蛋白家族的一种铁结合糖蛋白,存在于大多数生物体液中,是哺乳动物先天免疫系统的主要组成部分。其保护作用范围广泛,从对包括细菌、病毒、真菌和寄生虫在内的多种微生物的直接抗菌活性,到抗炎和抗癌活性。Lf之所以能产生如此众多的活性,是因为其作用机制不仅利用了Lf结合铁的能力,还涉及Lf与宿主和病原体的分子及细胞成分之间的相互作用。本章总结了我们目前对Lf结构-功能关系的理解,这些关系解释了Lf在宿主防御中的作用。