4.6 Review

Nutritional Immunity: S100 Proteins at the Host-Pathogen Interface

期刊

JOURNAL OF BIOLOGICAL CHEMISTRY
卷 290, 期 31, 页码 18991-18998

出版社

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R115.645085

关键词

-

资金

  1. United States Department of Veterans Affairs [1I01BX002482]
  2. National Institutes of Health [R01 AI101171, T32DK007673]
  3. Vanderbilt Digestive Disease Research Center (VDDRC) [P30DK058404]

向作者/读者索取更多资源

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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.6
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据