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(Received for publication, August 21, 1996, and in revised form, December 20, 1996)
From the Institut für Pharmakologie und Toxikologie der
Albert-Ludwigs-Universität Freiburg,
D-79104 Freiburg, Germany
Clostridium difficile toxin B that is
one of the largest cytotoxins (270 kDa) known acts on Rho subfamily
proteins by monoglucosylation (Just, I., Selzer, J., Wilm, M., von
Eichel-Streiber, C., Mann, M., and Aktories, K. (1995)
Nature 375, 500-503). By deletion analysis we identified
the enzyme and cytotoxic activity of the toxin to be located at the N
terminus of the holotoxin. A 63-kDa fragment of toxin B covering the
first 546 amino acid residues glucosylated Rho, Rac, and Cdc42, but not
Ras, by using UDP-glucose as a cosubstrate. As known for the holotoxin,
glucosylation by the toxin fragment was favored with the GDP-bound form
of the low molecular mass GTPases. Microinjection of the toxin fragment into NIH-3T3 cells induced rounding up of cells and redistribution of
the actin cytoskeleton. In contrast, a toxin fragment encompassing the
first 516 amino acid residues was at least 1000-fold less active than
toxin fragment 1-546 and cytotoxically inactive. The data give direct
evidence for location of the enzyme activity of C. difficile toxin B at the N-terminal 546 amino acids residues and
indicate a functionally and/or structurally important role of the
region from amino acid residues 516 through 546 for enzyme and
cytotoxic activities.
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