Nutritional Immunity: S100 Proteins at the Host-Pathogen Interface

被引：176
作者：
Zackular, Joseph P. [1 ]
Chazin, Walter J. [2 ,3 ,4 ]
Skaar, Eric P. [1 ]
机构：
[1] Vanderbilt Univ, Dept Pathol Microbiol & Immunol, Sch Med, Nashville, TN 37232 USA
[2] Vanderbilt Univ, Dept Biochem, Nashville, TN 37232 USA
[3] Vanderbilt Univ, Dept Chem, Nashville, TN 37232 USA
[4] Vanderbilt Univ, Struct Biol Ctr, Nashville, TN 37232 USA
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 2015年 / 290卷 / 31期
基金：
美国国家卫生研究院;
关键词：
CALCIUM-BINDING PROTEINS; MYELOID-RELATED PROTEINS; PSORIASIN S100A7; CARDIOVASCULAR-DISEASE; HUMAN CALPROTECTIN; CRYSTAL-STRUCTURES; SERUM-LEVELS; EXPRESSION; INFLAMMATION; ZINC;
D O I：
10.1074/jbc.R115.645085
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The S100 family of EF-hand calcium (Ca2+)-binding proteins is essential for a wide range of cellular functions. During infection, certain S100 proteins act as damage-associated molecular patterns (DAMPs) and interact with pattern recognition receptors to modulate inflammatory responses. In addition, these inflammatory S100 proteins have potent antimicrobial properties and are essential components of the immune response to invading pathogens. In this review, we focus on S100 proteins that exhibit antimicrobial properties through the process of metal limitation, termed nutritional immunity, and discuss several recent advances in our understanding of S100 protein-mediated metal sequestration at the site of infection.
引用
收藏
页码：18991 / 18998
页数：8
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