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Analysis of the complete sequence of a muscle calcium-binding protein of Schistosoma mansoni*

Published online by Cambridge University Press:  06 April 2009

T. J. Stewart ,
A. L. Smith  and
J. C. Havercroft
T. J. Stewart
Affiliation:
Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP
A. L. Smith
Affiliation:
Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP
J. C. Havercroft
Affiliation:
Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP
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Summary

The complete sequence of the cDNA encoding a 20 kDa calcium-binding protein of Schistosoma mansoni (Sm20) has been determined. The predicted amino acid sequence contains 4 EF hand domains but examination of the predicted secondary structure of Sm20, together with the specific residues in each calcium-binding domain, suggests that only 1 EF hand (domain IV) is functional. Sm20 is most homologous to calmodulin, troponin C and the regulatory light-chain of myosin, particularly those of invertebrates. However, troponin C and the regulatory light-chain of myosin can be distinguished from Sm20 by size and by their differential levels of expression during the life-cycle. Sm20 also appears to be distinct from calmodulin but may be functionally equivalent to the soluble sarcoplasmic calcium-binding proteins of molluscs and crustacea which may act as a reservoir for calcium in muscle. Sm20 is encoded by a small multi-gene family whose members are clustered within a 15 kb region of the genome. A 20 kDa antigen, cross-reactive with Sm20, is expressed in Schistosoma haematobium, Fasciola hepatica and Paragonomus mexicanus.

Keywords

Schistosoma mansonicalciummusclesequence.
Type
Research Article
Information
Parasitology , Volume 105 , Issue 3 , December 1992 , pp. 399 - 408
Copyright
Copyright © Cambridge University Press 1992

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