論文 - 詳細
| RRC ID | 43014 |
|---|---|
| 著者 | Jung YC, Mizuki E, Akao T, Côté JC. |
| タイトル | Isolation and characterization of a novel Bacillus thuringiensis strain expressing a novel crystal protein with cytocidal activity against human cancer cells. |
| ジャーナル | J Appl Microbiol |
| Abstract |
AIMS:To characterize a novel, unusual, Bacillus thuringiensis strain, to clone its Cry gene and determine the spectrum of action of the encoded Cry protein. METHODS AND RESULTS:The B. thuringiensis strain, referred to as M15, was isolated from dead two-spotted spider mites (Tetranychus urticae Koch; Arthropoda: Arachnida: Tetranychidae). It is an autoagglutination-positive strain and is therefore non-serotypeable. A sporulated culture produces a roughly spherical parasporal inclusion body, the crystal, tightly coupled to the spore. Although the crystal appears to be composed of at least two major polypeptides of 86 and 79 kDa as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Southern hybridization indicates that the corresponding crystal protein gene is likely present in only one copy. The crystal protein gene was cloned and, based on nucleotide sequence homology with an orthologous cry31Aa1 gene, assigned the name cry31Aa2. Although initially isolated from spider mites, B. thuringiensis M15 is non-toxic to spider mites and it does not produce the wide spectrum beta-exotoxin. Assays on mammalian cells, however, reveal that Cry31Aa2, when cleaved with trypsin, is cytocidal to some human cancer cells but not to normal human cells. No cytocidal activity was induced after protease treatment of Cry31Aa2 with either chymotrypsin or proteinase K. Trypsin, chymotrypsin and proteinase K cleavage sites were determined. CONCLUSIONS:The B. thuringiensis strain M15 exhibits specific cytocidal activities against some human cancer cells. SIGNIFICANCE AND IMPACT OF THE STUDY:This study raises questions as to the actual role of this bacterial strain and its crystal protein in the environment. It may be possible to further develop the Cry31Aa2 protein to target specific human cancer cells. |
| 巻・号 | 103(1) |
| ページ | 65-79 |
| 公開日 | 2007-7-1 |
| DOI | 10.1111/j.1365-2672.2006.03260.x |
| PII | JAM3260 |
| PMID | 17584453 |
| MeSH | Amino Acid Sequence Animals Antineoplastic Agents / metabolism Antineoplastic Agents / pharmacology* Bacillus thuringiensis / genetics Bacillus thuringiensis / isolation & purification Bacillus thuringiensis / metabolism* Bacillus thuringiensis / ultrastructure Bacillus thuringiensis Toxins Bacterial Proteins / genetics Bacterial Proteins / metabolism Bacterial Proteins / pharmacology* Bacterial Toxins / genetics Bacterial Toxins / metabolism Bacterial Toxins / pharmacology* Base Sequence Blotting, Southern Cell Survival / drug effects Dose-Response Relationship, Drug Electrophoresis, Polyacrylamide Gel / methods Endotoxins / genetics Endotoxins / metabolism Endotoxins / pharmacology* Gene Expression Genes, Bacterial Hemolysin Proteins / genetics Hemolysin Proteins / metabolism Hemolysin Proteins / pharmacology* Humans Molecular Sequence Data Tetranychidae / microbiology Tumor Cells, Cultured |
| IF | 3.066 |
| 引用数 | 29 |
| WOS 分野 | BIOTECHNOLOGY & APPLIED MICROBIOLOGY MICROBIOLOGY |
| リソース情報 | |
| ヒト・動物細胞 | HeLa(RCB0007) TCS(RCB0638) MOLT-4(RCB0206) HL60(RCB0041) Jurkat(RCB0806) MRC-5 A549(RCB0098) Hep G2 CACO-2(RCB0988) Vero(RCB0001) COS-7(RCB0539) NIH3T3 |