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ID 49252
JaLCDOI
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Thumnail 67_1_9.pdf 1.22 MB
Author
Fatmawati, Ni Nengah Dwi
Sakaguchi, Yoshihiko
Oda, Masataka
Shimizu, Kenta
Sakurai, Jun
Oguma, Keiji
Abstract
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.
Keywords
botulinum phospholipase C
botulinum toxin
phospholipase C activity
sphingomyelinase activity
hemolytic activity
Amo Type
Original Article
Published Date
2013-02
Publication Title
Acta Medica Okayama
Volume
volume67
Issue
issue1
Publisher
Okayama University Medical School
Start Page
9
End Page
18
ISSN
0386-300X
NCID
AA00508441
Content Type
Journal Article
language
英語
Copyright Holders
CopyrightⒸ 2013 by Okayama University Medical School
File Version
publisher
Refereed
True
PubMed ID
Web of Science KeyUT
Related Url
http://ousar.lib.okayama-u.ac.jp/metadata/49731