Identification of a new member of the PBAN family of neuropeptides from the fire ant, Solenopsis invicta

Authors

  • M.-Y. Choi,

    1. United States Department of Agriculture-Agriculture Research Service, Center of Medical, Agricultural and Veterinary Entomology (CMAVE), 1600 SW 23rd Dr. Gainesville, FL 32608, USA
    Search for more papers by this author
  • R. K. Vander Meer

    1. United States Department of Agriculture-Agriculture Research Service, Center of Medical, Agricultural and Veterinary Entomology (CMAVE), 1600 SW 23rd Dr. Gainesville, FL 32608, USA
    Search for more papers by this author

  • The cDNA sequence reported in this paper has been deposited in the GenBank database (Accession no. FJ223176)

Dr. Man-Yeon Choi, United States Department of Agriculture-Agriculture Research Service, Center of Medical, Agricultural and Veterinary Entomology (CMAVE), 1600 SW 23rd Dr. Gainesville, FL 32608, USA. Tel/Fax: 1-352-374-5818; e-mail: mychoi@ars.usda.gov and Dr. Robert K. Vander Meer e-mail: bob.vandermeer@ars.usda.gov

Abstract

Neuropeptide hormones produced by neurosecretory cells in the central or peripheral nervous systems regulate various physiological and behavioral events during insect development and reproduction. PBAN/Pyrokinin is a major neuropeptide family, characterized by a 5-amino-acid C-terminal sequence, FXPRLamide. This family of peptides has been implicated in regulating various physiological functions including, pheromone biosynthesis, muscle contraction, diapause induction or termination, melanization, and puparium formation in different insect species. In the present study, we report a new member of the PBAN family from the red imported fire ant, Solenopsis invicta, Soi-PBAN, composed of 26-AA (GSGEDLSYGDAYEVDEDDHPLFVPRL). Three additional peptides were deduced from Soi-PBAN cDNA: 15-AA (TSQDIASGMWFGPRL), 8-AA (QPQFTPRL) and 9-AA (LPWIPSPRL), that correspond to diapause hormone (DH), β-neuropeptide (NP), and γ-NP, which are found in many lepidopteran moths. Five peptides, DH, α, β, γ NPs, and PBAN are encoded from PBAN genes of lepidopteran moths, but in the fire ant the α-NP is missing. Each of the four synthetic peptides from the fire ant Soi-PBAN cDNA showed significant pheromonotropic activity in a moth model, indicating that these peptides are cross-reactive. Soi-β-NP induced the highest amount of pheromone production of the four peptides evaluated. The Soi-DH homologue had the lowest pheromonotropic activity, but was still significantly greater than control values. When the deduced amino acid sequences (entire ORF domains) from Soi-PBAN cDNA were compared with other known sequences, the fire ant was most similar to the honey bee, but phylogenetically distant from moth and beetle species. Soi-PBAN (26-AA) unlike the other three peptides shows a low degree of sequence identity with honeybee PBAN (33-AA). Based on the amino acid sequences encoded from insect PBAN genes identified to date, neuropeptide diversity is correlated with the taxonomic or phylogenetic classification of Insecta. From the present study we report the first neuropeptide identified and characterized from the central nervous system of Formicidae.

Ancillary