Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: June 4, 1998
Publication Date: N/A
A peptide family with a characteristic arginine-phenylalanine-amide C- terminal motif ("FMRFamide") and myoactive properties has been described for both free-living and animal parasitic nematodes. Primary structures reported to date probably represent only a fraction of those present in these animals, and their neuromodulatory nature suggests a potentially extensive involvement of this peptide family in the behavior, development and reproduction of nematodes. Immunocytochemical studies (Atkinson et al. 1988) detected the presence of FMRFamide-like peptides in the nervous system of the plant parasitic nematode Heterodera glycines, but no analyses of these peptides from plant parasitic nematodes have been available. We have developed methods for the collection and extraction of H. glycines and the detection of FMRFamide-like peptides using a competitive ELISA. HPLC-ELISA procedures reveal species-specific differences in the quality and quantity of FMRFamide-like peptides from H. glycines and the free-living nematodes Caenorhabditis elegans and Panagrellus redivivus. In addition, changes in FMRFamide-like peptide immunoreactivity were observed during H. glycines development and maturation. The significance of these developmental changes and species differences is discussed, and arguments for the involvement of FMRFamides in parasitic nematode growth and development are presented.