4.7 Article

Comprehensive Redox Profiling of the Thiol Proteome of Clostridium difficile

期刊

MOLECULAR & CELLULAR PROTEOMICS
卷 17, 期 5, 页码 1035-1046

出版社

ELSEVIER
DOI: 10.1074/mcp.TIR118.000671

关键词

-

资金

  1. Bundesministerium fur Bildung und Forschung [03Z1CN21]
  2. Niedersachsisches Ministerium fur Wissenschaft und Kultur [VWZN2889]
  3. Ministerium fur Bildung, Wissenschaft und Kultur Mecklenburg-Vorpommern [UG16001]
  4. University of Greifswald

向作者/读者索取更多资源

The strictly anaerobic bacterium C. difficile has become one of the most problematic hospital acquired pathogens and a major burden for health care systems. Although antibiotics work effectively in most C. difficile infections (CDIs), their detrimental effect on the intestinal microbiome paves the way for recurrent episodes of CDI. To develop alternative, non-antibiotics-based treatment strategies, deeper knowledge on the physiology of C. difficile, stress adaptation mechanisms and regulation of virulence factors is mandatory. The focus of this work was to tackle the thiol proteome of C. difficile and its stress-induced alterations, because recent research has reported that the amino acid cysteine plays a central role in the metabolism of this pathogen. We have developed a novel cysteine labeling approach to determine the redox state of protein thiols on a global scale. Applicability of this technique was demonstrated by inducing disulfide stress using the chemical diamide. The method can be transferred to any kind of redox challenge and was applied in this work to assess the effect of bile acids on the thiol proteome of C. difficile. We present redox-quantification for more than 1,500 thiol peptides and discuss the general difficulty of redox analyses of peptides possessing more than a single cysteine residue. The presented method will be especially useful not only when determining redox status, but also for providing information on protein quantity. Additionally, our comprehensive data set reveals protein cysteine sites particularly susceptible to oxidation and builds a groundwork for redox proteomics studies in C. difficile.

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

4.7
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