Yang, S. and Pyati, P. and Fitches, E. and Gatehouse, J.A. (2014) 'A recombinant fusion protein containing a spider toxin specific for the insect voltage-gated sodium ion channel shows oral toxicity towards insects of different orders.', Insect biochemistry and molecular biology., 47 . pp. 1-11.
Recombinant fusion protein technology allows specific insecticidal protein and peptide toxins to display activity in orally-delivered biopesticides. The spider venom peptide δ-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 μg 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.
|Keywords:||Neurotoxin, Insecticide, Recombinant protein expression system, Protein transport, Crop protection, Biotechnology.|
|Full text:||(VoR) Version of Record|
Available under License - Creative Commons Attribution.
Download PDF (1615Kb)
|Publisher Web site:||http://dx.doi.org/10.1016/j.ibmb.2014.01.007|
|Publisher statement:||© 2014 The Authors. Published by Elsevier Ltd. Open access under CC BY license.|
|Date accepted:||21 January 2014|
|Date deposited:||08 May 2015|
|Date of first online publication:||April 2014|
|Date first made open access:||No date available|
|Social bookmarking:||Export: EndNote, Zotero | BibTex|
|Look up in GoogleScholar | Find in a UK Library|