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ID 49252
JaLCDOI
フルテキストURL
Thumnail 67_1_9.pdf 1.22 MB
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
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
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
Oguma, Keiji Department of Bacteriology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
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.
キーワード
botulinum phospholipase C
botulinum toxin
phospholipase C activity
sphingomyelinase activity
hemolytic activity
Amo Type
Original Article
発行日
2013-02
出版物タイトル
Acta Medica Okayama
67巻
1号
出版者
Okayama University Medical School
開始ページ
9
終了ページ
18
ISSN
0386-300X
NCID
AA00508441
資料タイプ
学術雑誌論文
言語
English
著作権者
CopyrightⒸ 2013 by Okayama University Medical School
論文のバージョン
publisher
査読
有り
PubMed ID
Web of Science KeyUT
関連URL
http://ousar.lib.okayama-u.ac.jp/metadata/49731