Isolation and primary structure of neuropeptides from the mosquito, Aedes aegypti, immunoreactive to FMRFamide antiserum

Published

Journal Article

Two novel neuropeptides, Aea-HP-I and II, have been isolated from a head extract of the mosquito, Aedes aegypti; they were detected by a FMRFamide radioimmunoassay. The peptides were purified by gel filtration, ion exchange chromatography, and reversed-phase high performance liquid chromatography. Amino acid composition and sequence analysis, combined with enzymatic digestion, established the primary structure of Aea-HP-I as pGlu-Arg-Pro-Hyp-Ser-Leu-Lys-Thr-Arg-Phe-NH2 and Aea-HP-II as Thr-Arg-Phe-NH2. Aea-HP-I was synthesized, and chromatographic properties of the synthetic peptide were the same as those of the native peptide, thus confirming the structural analysis. The peptide has three unusual residues: an amino-terminal pGlu, a Hyp in the fourth position, and a carboxyl-terminal amide. The Pro-Hyp sequence occurs in toxin peptides from the venoms of cone snails and wasps and in bradykinin analogues. Although the functions of Aea-HP-I and II have not been determined, the peptides have the same RFa sequence at the carboxyl-terminal as Lem-SK-I and II (leucosulfakinins) and Lem-MS (leucomyosuppressin) in cockroaches and FMRFamide-related peptides in molluscs. © 1989.

Full Text

Duke Authors

Cited Authors

  • Matsumoto, S; Brown, MR; Crim, JW; Vigna, SR; Lea, AO

Published Date

  • January 1, 1989

Published In

Volume / Issue

  • 19 / 3

Start / End Page

  • 277 - 283

International Standard Serial Number (ISSN)

  • 0020-1790

Digital Object Identifier (DOI)

  • 10.1016/0020-1790(89)90073-5

Citation Source

  • Scopus