期刊
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
卷 47, 期 -, 页码 1-11出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.ibmb.2014.01.007
关键词
Neurotoxin; Insecticide; Recombinant protein expression system; Protein transport; Crop protection; Biotechnology
资金
- Technology Strategy Board (TSB) [TS/I000690/1]
- BBSRC China Partnership Scheme [BB/G530409]
- China Scholarship Scheme
- Durham University Doctoral Studentship
- EPSRC [TS/I000690/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [TS/I000690/1] Funding Source: researchfish
Recombinant fusion protein technology allows specific insecticidal protein and peptide toxins to display activity in orally-delivered biopesticides. The spider venom peptide delta-amaurobitoxin-PI1a, which targets insect voltage-gated sodium channels, was fused to the carrier snowdrop lectin (GNA) to confer oral toxicity. The toxin itself (PI1a) and an amaurobitoxin/GNA fusion protein (PI1a/GNA) were produced using the yeast Pichia pastoris as expression host. Although both proteins caused mortality when injected into cabbage moth (Mamestra brassicae) larvae, the PI1a/GNA fusion was approximately 6 times as effective as recombinant PI1a on a molar basis. PI1a alone was not orally active against cabbage moth larvae, but a single 30 mu g dose of the PI1a/GNA fusion protein caused 100% larval mortality within 6 days when fed to 3rd instar larvae, and caused significant reductions in survival, growth and feeding in 4th - 6th instar larvae. Transport of fusion protein from gut contents to the haemolymph of cabbage moth larvae, and binding to the nerve chord, was shown by Western blotting. The PI1a/GNA fusion protein also caused mortality when delivered orally to dipteran (Musca domestica; housefly) and hemipteran (Acyrthosiphon pisum; pea aphid) insects, making it a promising candidate for development as a biopesticide. (C) 2014 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据