2013年2月
Phospholipase C Produced by Clostridium botulinum Types C and D: Comparison of Gene, Enzymatic, and Biological Activities with Those of Clostridium perfringens Alpha-toxin
Acta Medica Okayama
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- 巻
- 67
- 号
- 1
- 開始ページ
- 9
- 終了ページ
- 18
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.18926/AMO/49252
- 出版者・発行元
- Okayama University Medical School
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.
- リンク情報
- ID情報
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- DOI : 10.18926/AMO/49252
- ISSN : 0386-300X
- CiNii Articles ID : 120005232332
- CiNii Books ID : AA00508441