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