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Immunolocalization of the fatty acid-binding protein Sj-FABPc within adult Schistosoma japonicum

Published online by Cambridge University Press:  01 July 1997

G. N. GOBERT ,
D. J. STENZEL ,
M. K. JONES  and
D. P. McMANUS
G. N. GOBERT
Affiliation:
Analytical Electron Microscopy Facility, Queensland University of Technology, GPO Box 2434, George Street, Brisbane, Queensland 4001, Australia
D. J. STENZEL
Affiliation:
Analytical Electron Microscopy Facility, Queensland University of Technology, GPO Box 2434, George Street, Brisbane, Queensland 4001, Australia
M. K. JONES
Affiliation:
Centre for Microscopy and Microanalysis, The University of Queensland, St Lucia, Brisbane, Queensland 4072, Australia
D. P. McMANUS
Affiliation:
Australian Centre for International and Tropical Health and Nutrition, Queensland Institute of Medical Research, 300 Herston Road, Herston, Brisbane, Queensland 4029, Australia
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Abstract

This paper describes the first localization study of the 14·7 kDa fatty acid-binding protein in Schistosoma japonicum (Sj-FABPc) using transmission electron microscopy. A polyclonal antibody raised against recombinant Sj-FABPc was used in combination with a colloidal gold marker to determine the distribution of the protein within adult parasites. Sj-FABPc was localized within lipid droplets below the subtegumental region of the male parasite. Additionally, Sj-FABPc was present in the vitelline droplets of the vitelline glands of female parasites. There were no detectable levels of Sj-FABPc on the surface or within the tegument of male or female parasites. Possible functions of Sj-FABPc within S. japonicum and the relevance of these immunolocalization findings in light of the recent reports that the homologue Sm-FABPc is an important anti-S. mansoni vaccine target molecule are also discussed.

Keywords

Schistosoma japonicumFABPcelectron microscopyimmunolocalizationcryopreparationvitelline glands
Type
Research Article
Information
Parasitology , Volume 115 , Issue 1 , July 1997 , pp. 33 - 39
Copyright
1997 Cambridge University Press

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