2010 Fiscal Year Final Research Report
Analysis of the interaction of Clostridium perfringens enterotoxin with claudin
| Project/Area Number |
21790418
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Bacteriology (including Mycology)
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| Research Institution | Osaka University |
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Principal Investigator |
TOSHIMA Hirono Osaka University, 微生物病研究所, 特任研究員 (10400532)
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| Project Period (FY) |
2009 – 2010
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| Keywords | 細菌毒素 / ウエルシュ菌 / クローディン |
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| Research Abstract |
Clostridium perfringens enterotoxin (CPE), a causative agent of food poisoning, is a pore-forming toxin. Claudin, a component of tight junctions, is a tetratransmembrane protein and constitutes a large family of more than 20 members, not all of which serve as the receptor for CPE. The mechanism by which the toxin distinguishes the sensitive claudins is unknown. In this study, we localized the region of claudin responsible for interaction with CPE to the C-terminal 12 amino acids of the second extracellular loop and found that an electrostatic attraction between the basic claudin region and the acidic CPE cleft is involved in their interaction. Furthermore, we present the structure of CPE determined by X-ray crystallography at 2.0 Å. These structural features imply that CPE is a β pore-forming toxin.
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[Journal Article] Crystal structure of Clostridium perfringens enterotoxin displays features of {beta}-pore-forming toxins.2011
Author(s)
Kengo Kitadokoro, Kousuke Nishimura, Shigeki Kamitani, Aya Fukui-Miyazaki, Hirono Toshima, Hiroyuki Abe, Yoichi Kamata, Yoshiko Sugita-Konishi, Shigeki Yamamoto, Hajime Karatani, Yasuhiko Horiguchi
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Journal Title
J Biol Chem doi:10.1074/jbc.
Pages: M111/228478
Peer Reviewed
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[Journal Article] Clostridium perfringens Enterotoxin Interacts with Claudins via Electrostatic Attraction.2010
Author(s)
Jun Kimura, Hiroyuki Abe, Shigeki Kamitani, Hirono Toshima, Aya Fukui, Masami Miyake, Yoichi Kamata, Yoshiko Sugita-onishi, Shigeki Yamamoto, Yasuhiko Horiguchi
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Journal Title
J Biol Chem VOL.285, NO.1
Pages: 401-408
Peer Reviewed
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