Part:BBa_K1974020
Snowdrop lectin+linker+6X His-Tag
Introduction:
Snowdrop (Galanthus nivalis) lectin is a protein that has special affinity to the glycoprotein on the surface of insect epithelial cells. According to reference, snowdrop-lectin is resistant to high temperature and would not be degraded by digestive juice. The species-specificity is based on the toxin, and the snowdrop lectin is the role of the carrier. When it is ligated by Pantide, which can increase the oral activity of Pantide.
GreatBay-SCIE 2024
This year, GreatBay-SCIE intergrate Galanthus nivalis agglutinin (GNA) into our experiment design. GNA is used for enhancing the oral and contact toxicity of the expressed mite and spider venom peptides (MVPs/SVPs). We constructed the plasmid pET28a-G1M5-His-SUMO-MVP/SVP-GNA-His (the MVPs can be PpVP2S, PpVP1S, or PpVP1F; the SVPs can be rCtx-4, Cs1A or HxTx-Hv1h). According to the toxicity bioassay, the MVP/SVP-GNA fusion proteins exhibit high contact efficacy. PpVP2S, a novel MVP we discovered by ourselves through conducting gene mining, achieves a spider mite mortality rate of 100% in 48 hours.
Reference
1. Elaine Fitches, Martin G. Edwards, Christopher Mee, Eugene Grishin, Angharad M. R. Gatehouse, John P. Edwards, John A. Gatehouse “Fusion proteins containing insect-specific toxins as pest control agents: snowdrop lectin delivers fused insecticidal spider venom toxin to insect haemolymph following oral ingestion,” Journal of Insect Physiology, 2004, 50, pp.61-71
2. Elaine C. Fitches, Prashant Pyati, Glenn F. King, John A. Gatehouse, “ Fusion to Snowdrop Lectin Magnifies the Oral Activity of Insecticidal Omega-Hexatoxin-Hv1a Peptide by Enabling Its Delivery to the Central Nervous System,”
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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