Roles of the carboxy-terminal region of Clostridium perfringens alpha toxin

Masahiro Nagahama; Hiroshi Iida; Eri Nishioka; Keinosuke Okamoto; Jun Sakurai

doi:10.1111/j.1574-6968.1994.tb07049.x

Roles of the carboxy-terminal region of Clostridium perfringens alpha toxin

Masahiro Nagahama, Hiroshi Iida, Eri Nishioka, Keinosuke Okamoto, Jun Sakurai

Research output: Contribution to journal › Article › peer-review

16 Citations (Scopus)

Abstract

Treatment of Clostridium perfringens alpha toxin with aminopeptidase resulted in no effect on various activities of the toxin. Aminopeptidase did not hydrolyze the native toxin or the toxin treated with urea in the presence of EDTA. Treatment with carboxypeptidase for 30 min resulted in a 75% decrease in these activities. Incubation of the native toxin with carboxypeptidase for 30 min released approximately 15 amino acids from the C-terminus of the toxin. The biological activities of a mutant toxin lacking 20 C-terminal residues of the toxin (AT_1-350) showed about 59-87% of the activity of native toxin. The mutant toxin showed partial antigenic identity with the native toxin. These data suggest that the C-terminal domain contributes to maintaining the active form of the toxin.

Original language	English
Pages (from-to)	297-301
Number of pages	5
Journal	FEMS Microbiology Letters
Volume	120
Issue number	3
DOIs	https://doi.org/10.1111/j.1574-6968.1994.tb07049.x
Publication status	Published - Jul 15 1994
Externally published	Yes

Keywords

Alpha toxin
Aminopeptidase
C-terminus
Carboxypeptidase
Clostridium perfringens
N-terminus

ASJC Scopus subject areas

Microbiology
Molecular Biology
Genetics

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10.1111/j.1574-6968.1994.tb07049.x

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title = "Roles of the carboxy-terminal region of Clostridium perfringens alpha toxin",

abstract = "Treatment of Clostridium perfringens alpha toxin with aminopeptidase resulted in no effect on various activities of the toxin. Aminopeptidase did not hydrolyze the native toxin or the toxin treated with urea in the presence of EDTA. Treatment with carboxypeptidase for 30 min resulted in a 75% decrease in these activities. Incubation of the native toxin with carboxypeptidase for 30 min released approximately 15 amino acids from the C-terminus of the toxin. The biological activities of a mutant toxin lacking 20 C-terminal residues of the toxin (AT1-350) showed about 59-87% of the activity of native toxin. The mutant toxin showed partial antigenic identity with the native toxin. These data suggest that the C-terminal domain contributes to maintaining the active form of the toxin.",

keywords = "Alpha toxin, Aminopeptidase, C-terminus, Carboxypeptidase, Clostridium perfringens, N-terminus",

author = "Masahiro Nagahama and Hiroshi Iida and Eri Nishioka and Keinosuke Okamoto and Jun Sakurai",

note = "Funding Information: This research was supported in part by a grant from the Ministry of Education, Sciences and Culture of Japan.",

year = "1994",

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doi = "10.1111/j.1574-6968.1994.tb07049.x",

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AU - Nagahama, Masahiro

AU - Iida, Hiroshi

AU - Nishioka, Eri

AU - Okamoto, Keinosuke

AU - Sakurai, Jun

N1 - Funding Information: This research was supported in part by a grant from the Ministry of Education, Sciences and Culture of Japan.

PY - 1994/7/15

Y1 - 1994/7/15

N2 - Treatment of Clostridium perfringens alpha toxin with aminopeptidase resulted in no effect on various activities of the toxin. Aminopeptidase did not hydrolyze the native toxin or the toxin treated with urea in the presence of EDTA. Treatment with carboxypeptidase for 30 min resulted in a 75% decrease in these activities. Incubation of the native toxin with carboxypeptidase for 30 min released approximately 15 amino acids from the C-terminus of the toxin. The biological activities of a mutant toxin lacking 20 C-terminal residues of the toxin (AT1-350) showed about 59-87% of the activity of native toxin. The mutant toxin showed partial antigenic identity with the native toxin. These data suggest that the C-terminal domain contributes to maintaining the active form of the toxin.

AB - Treatment of Clostridium perfringens alpha toxin with aminopeptidase resulted in no effect on various activities of the toxin. Aminopeptidase did not hydrolyze the native toxin or the toxin treated with urea in the presence of EDTA. Treatment with carboxypeptidase for 30 min resulted in a 75% decrease in these activities. Incubation of the native toxin with carboxypeptidase for 30 min released approximately 15 amino acids from the C-terminus of the toxin. The biological activities of a mutant toxin lacking 20 C-terminal residues of the toxin (AT1-350) showed about 59-87% of the activity of native toxin. The mutant toxin showed partial antigenic identity with the native toxin. These data suggest that the C-terminal domain contributes to maintaining the active form of the toxin.

KW - Alpha toxin

KW - Aminopeptidase

KW - C-terminus

KW - Carboxypeptidase

KW - Clostridium perfringens

KW - N-terminus

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Roles of the carboxy-terminal region of Clostridium perfringens alpha toxin

Abstract

Keywords

ASJC Scopus subject areas

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