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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Agriculture / Faculty of Agriculture >
Peer-reviewed Journal Articles, etc >
Activation process of the mosquitocidal δ-endotoxin Cry39A produced by Bacillus thuringiensis subsp aizawai BUN1-14 and binding property to Anopheles stephensi BBMV
| Title: | Activation process of the mosquitocidal δ-endotoxin Cry39A produced by Bacillus thuringiensis subsp aizawai BUN1-14 and binding property to Anopheles stephensi BBMV |
| Authors: | Ito, Takeshi Browse this author | | Bando, Hisanori Browse this author →KAKEN DB | | Asano, Shin-ichiro Browse this author →KAKEN DB |
| Keywords: | Bacillus thuringiensis | | δ-Endotoxin | | Anopheles stephensi | | Processing | | Mosquito | | BBMV |
| Issue Date: | Sep-2006 |
| Publisher: | Elsevier B.V. |
| Journal Title: | Journal of Invertebrate Pathology |
| Volume: | 93 |
| Issue: | 1 |
| Start Page: | 29 |
| End Page: | 35 |
| Publisher DOI: | 10.1016/j.jip.2006.05.007 |
| PMID: | 16837008 |
| Abstract: | Most δ-endotoxins produced by Bacillus thuringiensis require proteolytic processing in order to become active. The in vitro and in vivo activation processes of Cry39A, a δ-endotoxin that is highly toxic to Anopheles stephensi, were investigated. Cry39A with a molecular mass of 72 kDa was processed in vitro into a 60 kDa fragment by trypsin and gut extract from A. stephensi larvae. N-terminal amino acid sequencing of the 60 kDa fragment revealed that trypsin and the protease(s) in the gut extract cleaved Cry39A between Arg61 and Gly62. In contrast, 40 and 25 kDa polypeptides were generated in vivo by intramolecular cleavage of the 60 kDa fragment in A. stephensi larvae. Further, a co-precipitation assay was used to investigate the binding property of the activated Cry39A to A. stephensi BBMV. Cry39A bound to A. stephensi BBMV specifically and did not compete with the Cry4Aa toxin. This indicated that the binding molecule(s) for Cry39A might differ from those for Cry4A. In addition, Cry39A preferentially bound to the Triton X-100-insoluble membrane fraction. |
| Relation: | http://www.sciencedirect.com/science/journal/00222011 |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/14743 |
| Appears in Collections: | 農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 浅野 眞一郎
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