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An IgG (Fcγ,)-binding protein of Taenia crassiceps (Cestoda) exhibits sequence homology and antigenic similarity with schistosome paramyosin

Published online by Cambridge University Press:  06 April 2009

B. Kalinna  and
D. P. McManus
B. Kalinna
Affiliation:
Molecular Helminthology Laboratory, Division of Tropical Health and Infectious Diseases, Queensland Institute of Medical Research, The Bancroft Centre, 300 Herston Road, Herston, Brisbane, Queensland 4029, Australia
D. P. McManus
Affiliation:
Molecular Helminthology Laboratory, Division of Tropical Health and Infectious Diseases, Queensland Institute of Medical Research, The Bancroft Centre, 300 Herston Road, Herston, Brisbane, Queensland 4029, Australia
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Summary

Previous studies from this laboratory have suggested the presence of antibody-binding molecules on the surface of Taenia crassiceps metacestodes. We now report the purification of a T. crassiceps Fcγ -binding protein which has an equivalent molecular size (96 kDa), is antigenically similar and exhibits significant amino acid sequence homology to schistosome paramyosin. The similarities in molecular weight of the T. crassiceps protein, Schistosoma mansoni paramyosin and antigen B of T. solium, the close amino acid sequence homologies between the T. crassiceps protein and S. mansoni paramyosin and between S. mansoni paramyosin and antigen B of T. solium, and the antigenic similarity of the T. crassiceps protein with paramyosin indicates that this family of platyhelminth proteins are closely related. The known characteristics of T. solium antigen B (collagen binding affinity; disruption of complement function) and the Fcγ -binding activity of the T. crassiceps molecule suggests that this class of proteins may be multifunctional, fulfilling not only a structural role but also as components interacting with the host immune system to increase parasite survival.

Keywords

IgG-binding proteinFcγ-binding proteinTaenia crassicepsparamyosinamino acid sequencingaffinity chromatographyFPLC
Type
Research Article
Information
Parasitology , Volume 106 , Issue 3 , April 1993 , pp. 289 - 296
Copyright
Copyright © Cambridge University Press 1993

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