Proteolytic stabilization of a spider venom peptide results in an orally active bioinsecticide.

ABSTRACT:

Background

The toxin peptide U1-AGTX-Ta1b from the Hobo spider, Eratigena agrestis (Walckenaer, 1802), was studied to determine its potential to serve as a bioinsecticide.

Results

U1-AGTX-Ta1b has insecticidal potencies similar to commercial insecticides when injected directly into insect hemolymph but lacks activity when ingested by lepidopterans due to trypsin-like gut proteases. Alanine scanning identified an arginine and lysine rich patch on the peptide's surface that is critical for bioactivity. Targeted stability studies on these basic residues identified a single site, R9, to be the rate limiting site in U1-AGTX-Ta1b proteolysis. Mutation of position R9 to glutamine was sufficient to stabilize the peptide and render the toxin orally active with the additional benefit

SUBMITTER: Davis BR 

PROVIDER: S-EPMC12441774 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature