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J. Biol. Chem., Vol. 276, Issue 17, 13778-13783, April 27, 2001
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From the Activation of Clostridium
perfringens
Cleavage of a C-terminal Peptide Is Essential for Heptamerization
of Clostridium perfringens
-Toxin in the
Synaptosomal Membrane*
,,,, and¶
Department of Microbiology, Faculty of
Medicine, Kagawa Medical University, 1750-1 Miki-cho, Kita-gun, Kagawa
761-0793 and the § Department of Medical Technology, Kagawa
Prefectural College of Health Sciences, 281-1 Mure-cho, Kita-gun,
Kagawa 761-0123, Japan
-protoxin by tryptic digestion is accompanied by
removal of the 13 N-terminal and 22 C-terminal amino acid residues. In
this study, we examined the toxicity of four constructs: an
-protoxin derivative (PD), in which a factor Xa cleavage site was
generated at the C-terminal trypsin-sensitive site; PD without the 13 N-terminal residues (
N-PD); PD without the 23 C-terminal residues
(C-PD); and PD without either the N- or C-terminal residues
(NC-PD). A mouse lethality test showed that N-PD was inactive, as
is PD, whereas C-PD and NC-PD were equally active. C-PD and
NC-PD, but not the other constructs formed a large SDS-resistant
complex in rat synaptosomal membranes as demonstrated by
SDS-polyacrylamide gel electrophoresis. When NC-PD and C-PD, both
labeled with 32P and mixed in various ratios, were
incubated with membranes, eight distinct high molecular weight bands
corresponding to six heteropolymers and two homopolymers were detected
on a SDS-polyacrylamide gel, indicating the active toxin forms a
heptameric complex. These results indicate that C-terminal processing
is responsible for activation of the toxin and that it is essential for
its heptamerization within the membrane.
*
This work was supported by Grant-in-Aid from Japan Society
for the Promotion of Science.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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