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

页码：557 / 564

页数：8

共 50 条

[41] Cellular uptake of Clostridium botulinum C2 toxin:: Membrane translocation of a fusion toxin requires unfolding of its dihydrofolate reductase domain
Haug, G
Wilde, C
Leemhuis, J
Meyer, DK
Aktories, K
Barth, H
BIOCHEMISTRY, 2003, 42 (51) : 15284 - 15291
[42] Chloroquine derivatives block the translocation pores and inhibit cellular entry of Clostridium botulinum C2 toxin and Bacillus anthracis lethal toxin
Kreidler, Anna-Maria
Benz, Roland
Barth, Holger
ARCHIVES OF TOXICOLOGY, 2017, 91 (03) : 1431 - 1445
[43] Chloroquine derivatives block the translocation pores and inhibit cellular entry of Clostridium botulinum C2 toxin and Bacillus anthracis lethal toxin
Anna-Maria Kreidler
Roland Benz
Holger Barth
Archives of Toxicology, 2017, 91 : 1431 - 1445
[44] EGA Protects Mammalian Cells from Clostridium difficile CDT, Clostridium perfringens Iota Toxin and Clostridium botulinum C2 Toxin
Schnell, Leonie
Mittler, Ann-Katrin
Sadi, Mirko
Popoff, Michel R.
Schwan, Carsten
Aktories, Klaus
Mattarei, Andrea
Tehran, Domenico Azarnia
Montecucco, Cesare
Barth, Holger
TOXINS, 2016, 8 (04):
[45] The binary Clostridium botulinum C2 toxin:: Interaction of toxin components C2I and C2II
Barth, H
Roebling, R
Fritz, M
Hochmann, H
Aktories, K
NAUNYN-SCHMIEDEBERGS ARCHIVES OF PHARMACOLOGY, 2002, 365 : R4 - R4
[46] ADP-ribosylation of actin by the Clostridium botulinum C2 toxin in mammalian cells results in delayed caspase-dependent apoptotic cell death
Heine, Karin
Pust, Sascha
Enzenmueller, Stefanie
Barth, Holger
INFECTION AND IMMUNITY, 2008, 76 (10) : 4600 - 4608
[47] A PCR approach to determine the distribution of toxin genes in closely related Clostridium species:: Clostridium botulinum type C and D neurotoxins and C2 toxin, and Clostridium novyi α toxin
Heffron, Ann
Poxton, Ian R.
JOURNAL OF MEDICAL MICROBIOLOGY, 2007, 56 (02) : 196 - 201
[48] Clostridium botulinum C2 toxin as a molecular trojan horse for drug delivery
Fahrer, J.
Plunien, R.
Funk, J.
Lillich, M.
Barth, H.
NAUNYN-SCHMIEDEBERGS ARCHIVES OF PHARMACOLOGY, 2010, 381 : 78 - 78
[49] DIFFERENT TYPES OF ADP-RIBOSE PROTEIN BONDS FORMED BY BOTULINUM C2 TOXIN, BOTULINUM ADP-RIBOSYLTRANSFERASE C-3 AND PERTUSSIS TOXIN
AKTORIES, K
JUST, I
ROSENTHAL, W
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1988, 156 (01) : 361 - 367
[50] Characterization of the catalytic site of the ADP-ribosyltransferase Clostridium botulinum C2 toxin by site-directed mutagenesis
Barth, H
Preiss, JC
Hofmann, F
Aktories, K
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (45) : 29506 - 29511

← 1 2 3 4 5 →