Outputs (6)

Heterologous production of the insecticidal pea seed albumin PA1 protein by Pichia pastoris and protein engineering to potentiate aphicidal activity via fusion to snowdrop lectin Galanthus nivalis agglutinin; GNA) (2023)
Journal Article
De-Thier, J. S., Pyati, P., Bell, J., Readshaw, J. J., Brown, A. P., & Fitches, E. C. (2023). Heterologous production of the insecticidal pea seed albumin PA1 protein by Pichia pastoris and protein engineering to potentiate aphicidal activity via fusion to snowdrop lectin Galanthus nivalis agglutinin; GNA). Microbial Cell Factories, 22(1), Article 157. https://doi.org/10.1186/s12934-023-02176-1

Background
New bioinsecticides with novel modes of action are urgently needed to minimise the environmental and safety hazards associated with the use of synthetic chemical pesticides and to combat growing levels of pesticide resistance. The pea see... Read More about Heterologous production of the insecticidal pea seed albumin PA1 protein by Pichia pastoris and protein engineering to potentiate aphicidal activity via fusion to snowdrop lectin Galanthus nivalis agglutinin; GNA).

Enhancing the oral and topical insecticidal efficacy of a commercialized spider venom peptide biopesticide via fusion to the carrier snowdrop lectin (Galanthus nivalis agglutinin) (2022)
Journal Article
Sukiran, N. A., Pyati, P., Willis, C. E., Brown, A. P., Readshaw, J. J., & Fitches, E. C. (2023). Enhancing the oral and topical insecticidal efficacy of a commercialized spider venom peptide biopesticide via fusion to the carrier snowdrop lectin (Galanthus nivalis agglutinin). Pest Management Science, 79(1), 284-294. https://doi.org/10.1002/ps.7198

BACKGROUND: Spear®-T sold as a contact foliar spray for the control of glasshouse pests such as aphids, thrips, spider mites and whiteflies, contains the recombinant spider venom peptide GS-ω/κ-HxTx-Hv1h (named as GS-ω/κ-HxTx-Hv1a by Vestaron) as the... Read More about Enhancing the oral and topical insecticidal efficacy of a commercialized spider venom peptide biopesticide via fusion to the carrier snowdrop lectin (Galanthus nivalis agglutinin).

Recombinant Lectin from Tepary Bean (Phaseolus acutifolius) with Specific Recognition for Cancer-Associated Glycans: Production, Structural Characterization, and Target Identification (2020)
Journal Article
Martínez-Alarcón, D., Varrot, A., Fitches, E., Gatehouse, J. A., Cao, M., Pyati, P., Blanco-Labra, A., & Garcia-Gasca, T. (2020). Recombinant Lectin from Tepary Bean (Phaseolus acutifolius) with Specific Recognition for Cancer-Associated Glycans: Production, Structural Characterization, and Target Identification. Biomolecules, 10(4), Article 654. https://doi.org/10.3390/biom10040654

Herein, we report the production of a recombinant Tepary bean lectin (rTBL-1), its three-dimensional (3D) structure, and its differential recognition for cancer-type glycoconjugates. rTBL-1 was expressed in Pichia pastoris, yielding 316 mg per liter... Read More about Recombinant Lectin from Tepary Bean (Phaseolus acutifolius) with Specific Recognition for Cancer-Associated Glycans: Production, Structural Characterization, and Target Identification.

Optimising expression of the recombinant fusion protein biopesticide ω-hexatoxin-Hv1a /GNA in Pichia pastoris: Sequence modifications and a simple method for the generation of multi-copy strains (2014)
Journal Article
Pyati, P., Fitches, E., & Gatehouse, J. (2014). Optimising expression of the recombinant fusion protein biopesticide ω-hexatoxin-Hv1a /GNA in Pichia pastoris: Sequence modifications and a simple method for the generation of multi-copy strains. Journal of Industrial Microbiology and Biotechnology, 41(8), 1237-1247. https://doi.org/10.1007/s10295-014-1466-8

Production of recombinant protein bio-insecticides on a commercial scale can only be cost effective if host strains with very high expression levels are available. A recombinant fusion protein containing an arthropod toxin, ω-hexatoxin-Hv1a, (from fu... Read More about Optimising expression of the recombinant fusion protein biopesticide ω-hexatoxin-Hv1a /GNA in Pichia pastoris: Sequence modifications and a simple method for the generation of multi-copy strains.

Effect of insecticidal fusion proteins containing spider toxins targeting sodium and calcium ion channels on pyrethroid-resistant strains of peach-potato aphid (Myzus persicae) (2014)
Journal Article
Yang, S., Fitches, E., Pyati, P., & Gatehouse, J. (2015). Effect of insecticidal fusion proteins containing spider toxins targeting sodium and calcium ion channels on pyrethroid-resistant strains of peach-potato aphid (Myzus persicae). Pest Management Science, 71(7), 951-956. https://doi.org/10.1002/ps.3872

BACKGROUND: The recombinant fusion proteins Pl1a/GNA and Hv1a/GNA contain the spider venom peptides δ-amaurobitoxin-PI1a or ω-hexatoxin-Hv1a respectively, linked to snowdrop lectin (GNA). Pl1a targets receptor site 4 of insect voltage-gated sodium ch... Read More about Effect of insecticidal fusion proteins containing spider toxins targeting sodium and calcium ion channels on pyrethroid-resistant strains of peach-potato aphid (Myzus persicae).

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 (2014)
Journal Article
Yang, S., Pyati, P., Fitches, E., & Gatehouse, J. (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, 1-11. https://doi.org/10.1016/j.ibmb.2014.01.007

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, wa... Read More about 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.