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Toxins 2015, 7(2), 380-395;

Uptake of Clostridium botulinum C3 Exoenzyme into Intact HT22 and J774A.1 Cells

Institute of Toxicology, Hannover Medical School, Carl-Neuberg-Str. 1, Hannover D-30625, Germany
Author to whom correspondence should be addressed.
Academic Editor: Shin-ichi Miyoshi
Received: 12 December 2014 / Accepted: 22 January 2015 / Published: 2 February 2015
(This article belongs to the Section Bacterial Toxins)
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The Clostridium botulinum C3 exoenzyme selectively ADP-ribosylates low molecular weight GTP-binding proteins RhoA, B and C. This covalent modification inhibits Rho signaling activity, resulting in distinct actin cytoskeleton changes. Although C3 exoenzyme has no binding, the translocation domain assures that C3 enters cells and acts intracellularly. C3 uptake is thought to occur due to the high concentration of the C3 enzyme. However, recent work indicates that C3 is selectively endocytosed, suggesting a specific endocytotic pathway, which is not yet understood. In this study, we show that the C3 exoenzyme binds to cell surfaces and is internalized in a time-dependent manner. We show that the intermediate filament, vimentin, is involved in C3 uptake, as indicated by the inhibition of C3 internalization by acrylamide, a known vimentin disruption agent. Inhibition of C3 internalization was not observed by chemical inhibitors, like bafilomycin A, methyl-β-cyclodextrin, nocodazole or latrunculin B. Furthermore, the internalization of C3 exoenzyme was markedly inhibited in dynasore-treated HT22 cells. Our results indicate that C3 internalization depends on vimentin and does not depend strictly on both clathrin and caveolae. View Full-Text
Keywords: C3 exoenzyme; Clostridium botulinum; vimentin; dynasore; endocytosis C3 exoenzyme; Clostridium botulinum; vimentin; dynasore; endocytosis

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Rohrbeck, A.; von Elsner, L.; Hagemann, S.; Just, I. Uptake of Clostridium botulinum C3 Exoenzyme into Intact HT22 and J774A.1 Cells. Toxins 2015, 7, 380-395.

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