A Peptide Ligand for GPCR PBAN-R

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This review focuses on the endocrine regulation of reproductive behavior in moth species with particular emphasis on Helicoverpa spp. Reproductive behavior in most adult moths is dependent on the release of a unique blend of sex pheromones by the females to attract conspecific males. Mating, on the other hand, results in a loss of sexual receptivity due to the transfer of secretions from the male accessory glands, which renders females unattractive to ensuing mates. Synchronization of sexual behavior is attained by the timely release of Pheromone-Biosynthesis-Activating Neuropeptide (PBAN), a member of the PBAN/Pyrokinin neuropeptide family, characterized by a common amino acid sequence FXPRLamide motif in the C-terminus. PBAN is released into the hemolymph of females during the scotophase and is drastically reduced after mating, contributing to the loss in female receptivity. Pheromone production is age-dependent and Juvenile Hormone is involved in its regulation. PBAN activates pheromone production through its binding to a PBAN-Receptor (PBAN-R) and subsequent up-regulation of key enzymes in the biosynthetic pathway. The PBAN-R gene was identified as a member of the G-protein coupled receptor family (GPCRs), classified with the vertebrate subfamily of neuromedin U receptors. Using both biochemical and in silico mutagenesis studies, putative binding sites are predicted. Differential expression studies reveal its localization in pheromone glands, neural tissues and the male aedeagus. In the latter tissue, no activity and/or receptor-binding can be detected in response to PBAN. These results raise many questions concerning the evolutionary role of the PBAN/Pyrokinin receptors belonging to the GPCR family.

Rafaeli A. Pheromone biosynthesis activating neuropeptide (PBAN): regulatory role and mode of action. Gen Comp Endocrinol. 2009;162(1):69-78.

The pyrokinin/pheromone-biosynthesis-activating neuropeptide (PBAN) family of peptides found in insects is characterized by a 5-amino-acid C-terminal sequence, FXPRLamide. The pentapeptide is the active core required for diverse physiological functions, including the stimulation of pheromone biosynthesis in female moths, muscle contraction, induction of embryonic diapause, melanization, acceleration of puparium formation, and termination of pupal diapause. We have used immunocytochemical techniques to demonstrate the presence of pyrokinin/PBAN-like peptides in the central nervous system of the fire ant, Solenopsis invicta. Polyclonal antisera against the C-terminal end of PBAN have revealed the location of the peptide-producing cell bodies and axons in the central nervous system. Immunoreactive material is detectable in at least three groups of neurons in the subesophageal ganglion and corpora cardiaca of all adult sexual forms. The ventral nerve cord of adults consists of two segmented thoracic ganglia and four segmented abdominal ganglia. Two immunoreactive pairs of neurons are present in the thoracic ganglia, and three neuron pairs in each of the first three abdominal ganglia. The terminal abdominal ganglion has no immunoreactive neurons. PBAN immunoreactive material found in abdominal neurons appears to be projected to perisympathetic organs connected to the abdominal ganglia. These results indicate that the fire ant nervous system contains pyrokinin/PBAN-like peptides, and that these peptides are released into the hemolymph. In support of our immunocytochemical results, significant pheromonotropic activity is found in fire ant brain-subesophageal ganglion extracts from all adult fire ant forms (queens, female and male alates, and workers) when extracts are injected into decapitated females of Helicoverpa zea. This is the first demonstration of the presence of pyrokinin/PBAN-like peptides and pheromonotropic activity in an ant species.

Choi MY, Raina A, Vander meer RK. PBAN/pyrokinin peptides in the central nervous system of the fire ant, Solenopsis invicta. Cell Tissue Res. 2009;335(2):431-9.

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