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A pheromonotropic peptide of Helicoverpa zea , with melanizing activity, interaction with PBAN, and distribution of immunoreactivity
Author(s) -
Raina Ashok K.,
Kingan Timothy G.,
Kochansky Jan P.
Publication year - 2003
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.10094
Subject(s) - peptide , biology , peptide sequence , medicine , noctuidae , helicoverpa zea , amino acid , endocrinology , larva , microbiology and biotechnology , biochemistry , gene , botany
The sequence of an 18–amino acid residue peptide was deduced from the gene encoding PBAN and other peptides with common C‐termini in Helicoverpa zea . The peptide caused melanization in larvae and pheromone production in females of H. zea, and was designated pheromonotropic melanizing peptide (Hez‐PMP). The peptide has a 83% sequence homology with a pheromonotropic peptide isolated from Pseudaletia separata . PMP caused melanization and mortality when injected into larvae just before molting. Whereas intense melanization was caused with a dose of 1,000 pmol, peak mortality occurred at 100 pmol, with 50% of larvae dying within 48 h after injection. Pheromonotropic activity of PMP was dose dependent. Co‐injection of Hez‐PMP and Hez‐PBAN into a female resulted in suppression of the pheromonotropic effect of PBAN. Whole‐mount immunocytochemical studies revealed PMP‐like immunoreactivity in frontal ganglion, subesophageal, thoracic, and abdominal ganglia as well as the esophageal nerve. Arch. Insect Biochem. Physiol. 53:147–157, 2003. Published 2003 Wiley‐Liss, Inc.