Pheromonostatic peptide used to disrupt mating of the corn earworm, helicoverpa zea
AssigneeThe United States of America as represented by the Secretary of Agriculture
InventorsTimothy G. Kingan, Ashok K. Raina
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Abstract
A polypeptide having the property of rendering a female Helicoverpa zea moth non-receptive to mating was isolated from the reproductive tract of the male moth. The peptide is transferred from the male to the female during mating and causes a depletion of the female sex pheromone thereby resulting in a decline in sexual attractiveness for at least 24 hours. The peptide is referred to as pheromonostatic peptide, or PSP. It is a basic peptide having 57 amino acid residues, a molecular weight of 6617 daltons and contains one pair of cysteine residues in a disulfide linkage.
Claims3
An isolated polypeptide comprising the amino acid sequence:
- ##STR2## where X is pyro-GLU and Y is a mixture of ASN and ASP, and effective analogs and derivatives thereof.
Dependencies are inferred from the claim text.