Processing of Clostridium difficile toxins

被引：45

作者：

Giesemann, Torsten

Egerer, Martina

Jank, Thomas

Aktories, Klaus ^{[1
]}

机构：

[1] Univ Freiburg, Inst Expt, D-79104 Freiburg, Germany

来源：

JOURNAL OF MEDICAL MICROBIOLOGY | 2008年 / 57卷 / 06期

关键词：

D O I：

10.1099/jmm.0.47742-0

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The pathogenicity of Clostridium difficile depends on the large clostridial glucosylating toxins A and B (TcdA and TcdB). The proteins accomplish their own uptake by a modular structure comprising a catalytic and a binding/translocation domain. Based on a proteolytic processing step solely the catalytic domain reaches the cytosol. Within the cells, the glucosyltransferases inactivate small GTIPases by mono-O-glucosylation. Here, a short overview is given regarding latest insights into the intramolecular processing, which is mediated by an intrinsic protease activity.

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收藏

页码：690 / 696

页数：7

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