Isolation and identification of a pheromonotropic neuropeptide from the brain-suboesophageal ganglion complex of Lymantria dispar: a new member of the PBAN family.
A pheromonotropic peptide was isolated from brain-suboesophageal ganglion complexes of the adult female gypsy moth, Lymantria dispar, using a 5-step HPLC purification protocol and an in vivo bioassay in Helicoverpa zea. The intact peptide was sequenced by automated Edman degradation. The L. dispar pheromone biosynthesis activating neuropeptide (Lyd-PBAN) is a C-terminally amidated 33-amino acid peptide with a molecular weight of 3881. The peptide was synthesized using Fmoc procedures. Lyd-PBAN has sequence homology with Hez-PBAN (81.8%) and Bom-PBAN-I (66.7%). All three PBANs share the C-terminal hexapeptide sequence, Tyr-Phe-Ser-Pro-Arg-Leu-NH2. In addition, the C-terminal pentapeptide sequences of Pseudaletia pheromonotropin (Pss-PT), Bombyx diapause hormone (Bom-DH), the locustamyotropins (Lom-MT) and leucopyrokinin (Lem-PK) are identical or have a high degree of homology to the C-terminus of PBANs.
Masler
E P
EP
Insect Neurobiology and Hormone Laboratory, Plant Sciences Institute, USDA-ARS, Beltsville, MD 20705-2350.
Raina
A K
AK
Wagner
R M
RM
Kochansky
J P
JP
D000595:Amino Acid Sequence; D000818:Animals; D001923:Brain Chemistry; D002851:Chromatography, High Pressure Liquid; D004947:Esophagus / Q000294:innervation; D005260:Female; D017952:Ganglia, Invertebrate / Q000737:chemistry*; D008969:Molecular Sequence Data; D009036:Moths / Q000737:chemistry*; D009479:Neuropeptides / Q000737:chemistry / Q000302:isolation & purification*; D017386:Sequence Homology, Amino Acid; D012724:Sex Attractants / Q000737:chemistry / Q000302:isolation & purification*
D009479:Neuropeptides; D012724:Sex Attractants; C079709:pheromone biosynthesis activating neuropeptide, Helicoverpa zea; C090741:pheromone biosynthesis- activating neuropeptide, Lymantria