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J. Biol. Chem., Vol. 277, Issue 46, 43659-43666, November 15, 2002

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Clostridium perfringens Iota Toxin
MAPPING OF THE Ia DOMAIN INVOLVED IN DOCKING WITH Ib AND CELLULAR INTERNALIZATION^*

Jean-Christophe Marvaud, Bradley G. Stiles^§, Alexandre Chenal^¶, Daniel Gillet^¶, Maryse Gibert, Leonard A. Smith^§, and Michel R. Popoff

From the  CNR Anaérobies, Institut Pasteur, 75724 Paris Cedex 15, France, the ^§ Toxinology Division, United States Army Medical Research Institute of Infectious Diseases, Fort Detrick, Maryland 21702-5011, and the ^¶ Département d'Ingéniérie et d'Etudes des Protéines, CEA-Saclay, Gif sur yvette 91191, France

Clostridium perfringens iota toxin consists of two unlinked proteins. The binding component (Ib) is required to internalize into cells an enzymatic component (Ia) that ADP-ribosylates G-actin. To characterize the Ia domain that interacts with Ib, fusion proteins were constructed between the C. botulinum C3 enzyme, which ADP-ribosylates Rho, and various truncated versions of Ia. These chimeric molecules retained the wild type ADP-ribosyltransferase activity specific for Rho and were recognized by antibodies against C3 enzyme and Ia. Internalization of each chimera into Vero cells was assessed by measuring the disorganization of the actin cytoskeleton and intracellular ADP-ribosylation of Rho. Fusion proteins containing C3 linked to the C terminus of Ia were transported most efficiently into cells like wild type Ia in an Ib-dependent manner that was blocked by bafilomycin A1. The minimal Ia fragment that promoted translocation of Ia-C3 chimeras into cells consisted of 128 central residues (129-257). These findings revealed that iota toxin is a suitable system for mediating the entry of heterologous proteins such as C3 into cells.

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