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Comparative analyses of the neuropeptide F (NPF)- and FMRFamide-related peptide (FaRP)-immunoreactivities in Fasciola hepatica and Schistosoma spp

Published online by Cambridge University Press:  06 April 2009

N. J. Marks ,
D. W. Halton ,
A. G. Maule ,
G. P. Brennan ,
C. Shaw ,
V. R. Southgate  and
C. F. Johnston
N. J. Marks
Affiliation:
Comparative Neuroendocrinology Research Group, The Queen's University of Belfast, Belfast BT7 INN, UK
D. W. Halton
Affiliation:
Comparative Neuroendocrinology Research Group, The Queen's University of Belfast, Belfast BT7 INN, UK
A. G. Maule
Affiliation:
Comparative Neuroendocrinology Research Group, The Queen's University of Belfast, Belfast BT7 INN, UK
G. P. Brennan
Affiliation:
Comparative Neuroendocrinology Research Group, The Queen's University of Belfast, Belfast BT7 INN, UK
C. Shaw
Affiliation:
Comparative Neuroendocrinology Research Group, The Queen's University of Belfast, Belfast BT7 INN, UK
V. R. Southgate
Affiliation:
Department of Zoology, The Natural History Museum, London SW7 5BD, UK
C. F. Johnston
Affiliation:
Comparative Neuroendocrinology Research Group, The Queen's University of Belfast, Belfast BT7 INN, UK
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Summary

Immunochemical techniques were used to determine the distribution, chemical characteristics and relative abundance of immunoreactivity (IR) to two native platyhelminth neuropeptides, neuropeptide F (NPF) (Moniezia expansa) and the FMRFamide-related peptide (FaRP), GNFFRFamide, in the trematodes, Fasciola hepatica and Schistosoma mansoni; the larger S. margrebowiei was used in the chemical analysis. Extensive immunostaining for the two peptides was demonstrated throughout the nervous systems of both F. hepatica and S. mansoni, with strong IR also in the innervation of muscular structures, including those associated with the egg-forming apparatus. The patterns of immunostaining were similar to those previously described for the vertebrate neuropeptide Y superfamily of peptides and for FMRFamide. Ultra-structurally, gold labelling of NPF- and GNFFRFamide-IRs was localized exclusively to the contents of secretory vesicles in the axons and somatic cytoplasm of neurones. Double-labelling experiments showed an apparent homogeneity of antigenic sites, in all probability due to the demonstrated cross-reactivity of the FaRP antiserum with NPF. Radio-immunoassay of acid-ethanol extracts of the worms detected 8·3 pmol/g and 4·7 pmol/g equivalents of NPF- and FMRFamide-IRs, respectively, for F. hepatica, and corresponding values of 4·9 pmol/g and 4·3 pmol/g equivalents for S. margrebowiei. Gel-permeation chromatography resolved IR to both peptides in discrete peaks and these eluted in similar positions to synthetic NPF (M. expansa) and GNFFRFamide, respectively.

Keywords

Fasciola hepaticaSchistosoma mansoniS. margrebowieineuropeptide FFaRPsGNFFRFamideimmuno-cytochemistryimmunogold labellingradioimmunoassay
Type
Research Article
Information
Parasitology , Volume 110 , Issue 4 , May 1995 , pp. 371 - 381
Copyright
Copyright © Cambridge University Press 1995

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