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Neuropeptide F: a novel parasitic flatworm regulatory peptide from Moniezia expansa (Cestoda: Cyclophyllidea)

Published online by Cambridge University Press:  06 April 2009

A. G. Maule
Affiliation:
Comparative Neuroendocrinology Research Group, Schools of Biology and Biochemistry, The Queen's University of Belfast, Belfast BT7 1NN, UK
C. Shaw
Affiliation:
Comparative Neuroendocrinology Research Group, Schools of Clinical Medicine, The Queen's University of Belfast, Belfast BT7 1NN, UK
D. W. Halton
Affiliation:
Comparative Neuroendocrinology Research Group, Schools of Biology and Biochemistry, The Queen's University of Belfast, Belfast BT7 1NN, UK
L. Thim
Affiliation:
Novo Nordisk A/S, Bagsvaerd, Denmark
C. F. Johnston
Affiliation:
Comparative Neuroendocrinology Research Group, Schools of Clinical Medicine, The Queen's University of Belfast, Belfast BT7 1NN, UK
I. Fairweather
Affiliation:
Comparative Neuroendocrinology Research Group, Schools of Biology and Biochemistry, The Queen's University of Belfast, Belfast BT7 1NN, UK
K. D. Buchanan
Affiliation:
Comparative Neuroendocrinology Research Group, Schools of Clinical Medicine, The Queen's University of Belfast, Belfast BT7 1NN, UK

Summary

Using a C-terminally directed pancreatic polypeptide (PP) antiserum and immunocytochemical methods, PP-immuno-reactivity (IR) was localized throughout the central (CNS) and peripheral nervous systems (PNS) of the cestode, Moniezia expansa. In the CNS, immunostaining was evident in the paired cerebral ganglia (primitive brain), connecting commissure, and the paired longitudinal nerve cords that are cross-linked by numerous regular transverse connectives. The PNS was seen to consist of a fine anastomosing nerve-net of immunoreactive fibres, many of which were closely associated with reproductive structures. Radioimmunoassay of this peptide IR in acid-alcohol extracts of the worm measured 192·8 ng/g of PP–IR. HPLC analyses of the M. expansa PP–IR identified a single molecular form which was purified to homogeneity. Plasma desorption mass spectrometry (PDMS) of purified parasite peptide resolved a single peptide with a molecular mass of 4599±10 Da. Automated gas-phase Edman degradation identified a 39-amino acid peptide with a C-terminal phenyl-alaninamide. Examination of its primary structure shows that it displays significant sequence homology with the vertebrate neuropeptide Y superfamily, suggesting that this platyhelminth-derived peptide is the phylogenetic precursor. Neuropeptide F (M. expansa) is the first regulatory peptide to be fully sequenced from the phylum Platyhelminthes and may represent a member of an important new class of invertebrate neuropeptide.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1991

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