Next Article in Journal
Next Article in Special Issue
Previous Article in Journal
Previous Article in Special Issue
Toxins 2013, 5(1), 106-119; doi:10.3390/toxins5010106
Article

Difference in F-Actin Depolymerization Induced by Toxin B from the Clostridium difficile Strain VPI 10463 and Toxin B from the Variant Clostridium difficile Serotype F Strain 1470

1
, 1
, 2
 and 1,*
Received: 14 November 2012; in revised form: 14 December 2012 / Accepted: 28 December 2012 / Published: 11 January 2013
(This article belongs to the Special Issue Novel Properties of Well-Characterized Toxins)
View Full-Text   |   Download PDF [2810 KB, uploaded 11 January 2013]
Abstract: Clostridium difficile toxin A (TcdA) and toxin B (TcdB) are the causative agent of the C. difficile-associated diarrhea (CDAD) and its severe form, the pseudomembranous colitis (PMC). TcdB from the C. difficile strain VPI10463 mono-glucosylates (thereby inactivates) the small GTPases Rho, Rac, and Cdc42, while Toxin B from the variant C. difficile strain serotype F 1470 (TcdBF) specifically mono-glucosylates Rac but not Rho(A/B/C). TcdBF is related to lethal toxin from C. sordellii (TcsL) that glucosylates Rac1 but not Rho(A/B/C). In this study, the effects of Rho-inactivating toxins on the concentrations of cellular F-actin were investigated using the rhodamine-phalloidin-based F-actin ELISA. TcdB induces F-actin depolymerization comparable to the RhoA-inactivating exoenzyme C3 from C. limosum (C3-lim). In contrast, the Rac-glucosylating toxins TcdBF and TcsL did not cause F-actin depolymerization. These observations led to the conclusion that F-actin depolymerization depends on the toxin’s capability of glucosylating RhoA. Furthermore, the integrity of focal adhesions (FAs) was analyzed using paxillin and p21-activated kinase (PAK) as FA marker proteins. Paxillin dephosphorylation was observed upon treatment of cells with TcdB, TcdBF, or C3-lim. In conclusion, the Rho-inactivating toxins induce loss of cell shape by either F-actin depolymerization (upon RhoA inactivation) or the disassembly of FAs (upon Rac1 inactivation).
Keywords: Rho protein; mono-glucosylation; latrunculin B; C. botulinum C2 toxin; C. limosum exoenzyme C3 Rho protein; mono-glucosylation; latrunculin B; C. botulinum C2 toxin; C. limosum exoenzyme C3
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Export to BibTeX |
EndNote


MDPI and ACS Style

May, M.; Wang, T.; Müller, M.; Genth, H. Difference in F-Actin Depolymerization Induced by Toxin B from the Clostridium difficile Strain VPI 10463 and Toxin B from the Variant Clostridium difficile Serotype F Strain 1470. Toxins 2013, 5, 106-119.

AMA Style

May M, Wang T, Müller M, Genth H. Difference in F-Actin Depolymerization Induced by Toxin B from the Clostridium difficile Strain VPI 10463 and Toxin B from the Variant Clostridium difficile Serotype F Strain 1470. Toxins. 2013; 5(1):106-119.

Chicago/Turabian Style

May, Martin; Wang, Tianbang; Müller, Micro; Genth, Harald. 2013. "Difference in F-Actin Depolymerization Induced by Toxin B from the Clostridium difficile Strain VPI 10463 and Toxin B from the Variant Clostridium difficile Serotype F Strain 1470." Toxins 5, no. 1: 106-119.


Toxins EISSN 2072-6651 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert