ISOLATION AND IDENTIFICATION OF A PHEROMONOTROPIC NEUROPEPTIDE FROM THE BRAIN-SUBESOPHAGEAL GANGLION COMPLEX OF LYMANTRIA-DISPAR - A NEW MEMBER OF THE PBAN FAMILY

A pheromonotropic peptide was isolated from brain-suboesophageal gangl ion complexes of the adult female gypsy moth, Lymantria dispar, using a 5-step HPLC purification protocol and an in vivo bioassay in Helicov erpa zea. The intact peptide was sequenced by automated Edman degradat ion. The L. dispar pheromone biosynthesis activating neuropeptide (Lyd -PBAN) is a C-terminally amidated 33-amino acid peptide with a molecul ar weight of 3881. The peptide was synthesized using Fmoc procedures. Lyd-PBAN has sequence homology with Hez-PBAN (81.8%) and Bom-PBAN-I (6 6.7%). All three PBANs share the C-terminal hexapeptide sequence, Tyr- Phe-Ser-Pro-Arg-Leu-NH,. Tn addition, the C-terminal pentapeptide sequ ences 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 P BANs.