フルテキストURL ApplEntomolZool_52_1_61.pdf ApplEntomolZool_52_1_61_fig.pdf ApplEntomolZool_52_1_61_suppl.pdf
著者 Hayakawa, Tohru| Yoneda, Naoya| Okada, Kouji| Higaki, Ayuko| Mohammad Tofazzal Hossain Howlader| Ide, Toru|
抄録 A 2,175-bp modified gene (cry11Ba-S1) encoding Cry11Ba from Bacillus thuringiensis subsp. jegathesan was designed and the recombinant protein was expressed as a fusion protein with glutathione S-transferase in Escherichia coli. The recombinant Cry11Ba was highly toxic against Culex pipiens mosquito larvae, being nine and 17 times more toxic than mosquitocidal Cry4Aa and Cry11Aa from Bacillus thuringiensis subsp. israelensis, respectively. Interestingly, a further increase in the toxicity of the recombinant Cry11Ba was achieved by mixing with Cry4Aa, but not with Cry11Aa. These findings suggested that Cry11Ba worked synergistically with Cry4Aa, but not with Cry11Aa, in exhibiting toxicity against C. pipiens larvae. On the other hand, the amount of Cry toxin bound to brush border membrane vesicles (BBMVs) did not significantly change between individual toxins and the toxin mixtures, suggesting that the increase in toxins binding to BBMVs was not a reason for the observed synergistic effect. It is generally accepted that synergism of toxins is a potentially powerful tool for enhancing insecticidal activity and managing Cry toxin resistance in mosquitoes. The mixture of Cry4Aa and Cry11Ba in order to increase toxicity would be very valuable in terms of mosquito control.
キーワード Cry toxin Synergistic toxicity Insect pest control Biological control Disease vector
備考 This is an Accepted Manuscript of an article published by Springer Nature
発行日 2017-02
出版物タイトル Applied Entomology and Zoology
52巻
1号
出版者 Springer Japan
開始ページ 61
終了ページ 68
ISSN 0003-6862
NCID AA00543238
資料タイプ 学術雑誌論文
言語 English
OAI-PMH Set 岡山大学
論文のバージョン author
DOI 10.1007/s13355-016-0454-z
Web of Sience KeyUT 000394150200007
関連URL isVersionOf https://doi.org/10.1007/s13355-016-0454-z