Clostridium botulinum C2 toxin -: New insights into the cellular up-take of the actin-ADP-ribosylating toxin

被引：20
|
作者：
Aktories, K [1 ]
Barth, H [1 ]
机构：
[1] Univ Freiburg, Inst Expt & Klin Pharmakol & Toxikol, D-79104 Freiburg, Germany
来源：
INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY | 2004年 / 293卷 / 7-8期
关键词：
actin; ADP-ribosylation; bacterial toxin; chaperone; Hsp90; Clostridium botulinum C2 toxin; C. perfringens iota toxin;
D O I：
10.1078/1438-4221-00305
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
Clostridium botulinum C2 toxin is a member of the family of binary actin-ADP-ribosylating toxins. It consists of the enzyme component C2I, and the separated bind,ng/translocation component C2II. Proteolytically activated,C2II forms heptamers and binds to a carbohydrate cell surface receptor. After attachment of C2I, the toxin complex is endocytosed to reach early endosomes. At low pH of endosomes, C2II-heptamers insert into the membrane, form pores and deliver C2I into the cytosol. Here, C2I ADP-ribosylates actin at Arg177 to block actin polymerization and to induce depolymerization of actin filaments. The mini-review describes main properties of C2 toxin and discusses new findings on the involvement of chaperones in the up-take process of the toxin.
引用
收藏
页码：557 / 564
页数：8
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