JaLCDOI 10.18926/AMO/49252
フルテキストURL 67_1_9.pdf
著者 Fatmawati, Ni Nengah Dwi| Sakaguchi, Yoshihiko| Suzuki, Tomonori| Oda, Masataka| Shimizu, Kenta| Yamamoto, Yumiko| Sakurai, Jun| Matsushita, Osamu| Oguma, Keiji|
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 23439504
Web of Sience KeyUT 000316829900002
関連URL http://ousar.lib.okayama-u.ac.jp/metadata/49731