FullText URL K0004670.pdf K0004670_honbun.pdf
Author Fatmawati, Ni Nengah Dwi|
Published Date 2012-12-31
Content Type Thesis or Dissertation
Grant Number 甲第4670号
Granted Date 2012-12-31
Thesis Type 博士(医学)
Grantor 岡山大学
language 日本語 英語
JaLCDOI 10.18926/AMO/49252
FullText URL 67_1_9.pdf
Author Fatmawati, Ni Nengah Dwi| Sakaguchi, Yoshihiko| Suzuki, Tomonori| Oda, Masataka| Shimizu, Kenta| Yamamoto, Yumiko| Sakurai, Jun| Matsushita, Osamu| 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 23439504
Web of Sience KeyUT 000316829900002
Related Url http://ousar.lib.okayama-u.ac.jp/metadata/49731