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

• Published in: Insect biochemistry Vol. 19; no. 3; pp. 277 - 283
• Main Authors: Matsumoto, Shogo, Brown, Mark R., Crim, Joe W., Vigna, Steven R., Lea, Arden O.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier B.V 1989; New York, NY Pergamon Press
• Subjects: ACIDE AMINE; AEDES; AMINO ACID SEQUENCE; AMINO ACIDS; AMINOACIDOS; Biochemistry. Physiology. Immunology; Biological and medical sciences; BRADYKININ; CABEZA; CININA; Fundamental and applied biological sciences. Psychology; HEAD; HIDROXIPROLINA; HYDROXYPROLINE; Insecta; Invertebrates; KININE; KININS; NEUROHORMONE; Physiology. Development; TETE; bradykinin; insect; amino acid sequence; neurohormone; hydroxyproline; Purification; Molecular structure; Insecta; Blood sucking; HPLC chromatography; Primary structure; Neuropeptide; Arthropoda; Radioimmunoassay; Culicidae; Neurotransmitter; Aedes aegypti; Neurohormone; Invertebrata; FMRF amide; Diptera; Aminoacid sequence
• ISSN: 0020-1790
• DOI: 10.1016/0020-1790(89)90073-5

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-NH 2 and Aea-HP-II as Thr-Arg-Phe-NH 2. 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.