Journal
INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY
Volume 293, Issue 7-8, Pages 557-564Publisher
ELSEVIER GMBH
DOI: 10.1078/1438-4221-00305
Keywords
actin; ADP-ribosylation; bacterial toxin; chaperone; Hsp90; Clostridium botulinum C2 toxin; C. perfringens iota toxin
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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.
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