ID | 49252 |
JaLCDOI | |
フルテキストURL | |
著者 |
Fatmawati, Ni Nengah Dwi
Department of Bacteriology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Sakaguchi, Yoshihiko
Interdisciplinary Research Organization, Miyazaki University
Suzuki, Tomonori
Department of Bacteriology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Kaken ID
publons
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Oda, Masataka
Department of Microbiology, Faculty of Pharmaceutical Sciences, Tokushima Bunri University
Shimizu, Kenta
Shin-Nakamura Chemical Co., Ltd
Yamamoto, Yumiko
Department of Bacteriology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Kaken ID
publons
researchmap
Sakurai, Jun
Department of Microbiology, Faculty of Pharmaceutical Sciences, Tokushima Bunri University
Matsushita, Osamu
Department of Bacteriology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Kaken ID
researchmap
Oguma, Keiji
Department of Bacteriology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
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抄録 | Clostridium botulinum type C and D strains recently have been found to produce PLC on egg yolk agar plates. To characterize the gene, enzymatic and biological activities of C. botulinum PLCs (Cb-PLCs), the cb-plc genes from 8 strains were sequenced, and 1 representative gene was cloned and expressed as a recombinant protein. The enzymatic and hemolytic activities of the recombinant Cb-PLC were measured and compared with those of the Clostridium perfringens alpha-toxin. Each of the eight cb-plc genes encoded a 399 amino acid residue protein preceded by a 27 residue signal peptide. The protein consists of 2 domains, the N- and C-domains, and the overall amino acid sequence identity between Cb-PLC and alpha-toxin was greater than 50%, suggesting that Cb-PLC is homologous to the alpha-toxin. The key residues in the N-domain were conserved, whereas those in the C-domain which are important in membrane interaction were different than in the alpha-toxin. As expected, Cb-PLC could hydrolyze egg yolk phospholipid, p-nitrophenylphosphorylcholine, and sphingomyelin, and also exhibited hemolytic activity;however, its activities were about 4- to over 200-fold lower than those of alpha-toxin. Although Cb-PLC showed weak enzymatic and biological activities, it is speculated that Cb-PLC might play a role in the pathogenicity of botulism or for bacterial survival.
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キーワード | botulinum phospholipase C
botulinum toxin
phospholipase C activity
sphingomyelinase activity
hemolytic activity
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Amo Type | Original Article
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出版物タイトル |
Acta Medica Okayama
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発行日 | 2013-02
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巻 | 67巻
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号 | 1号
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出版者 | Okayama University Medical School
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開始ページ | 9
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終了ページ | 18
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ISSN | 0386-300X
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NCID | AA00508441
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資料タイプ |
学術雑誌論文
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言語 |
英語
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著作権者 | CopyrightⒸ 2013 by Okayama University Medical School
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論文のバージョン | publisher
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査読 |
有り
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PubMed ID | |
Web of Science KeyUT | |
関連URL | http://ousar.lib.okayama-u.ac.jp/metadata/49731
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