Characterisation of Sm20, a 20-kilodalton calcium-binding protein of Schistosoma mansoni

1990 ◽  
Vol 38 (2) ◽  
pp. 211-219 ◽  
Author(s):  
J HAVERCROFT ◽  
M HUGGINS ◽  
D DUNNE ◽  
D TAYLOR
1991 ◽  
Vol 13 (6) ◽  
pp. 593-604 ◽  
Author(s):  
J.C. HAVERCROFT ◽  
A.L. SMITH ◽  
R.H. WILLIAMS

Parasitology ◽  
1992 ◽  
Vol 105 (3) ◽  
pp. 399-408 ◽  
Author(s):  
T. J. Stewart ◽  
A. L. Smith ◽  
J. C. Havercroft

SUMMARYThe 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.


2008 ◽  
Vol 10 (6) ◽  
pp. 1373-1389 ◽  
Author(s):  
Ruchi Jain ◽  
Julien Santi-Rocca ◽  
Narendra Padhan ◽  
Sudha Bhattacharya ◽  
Nancy Guillen ◽  
...  

1976 ◽  
Vol 251 (15) ◽  
pp. 4744-4750 ◽  
Author(s):  
M A Brostrom ◽  
C O Brostrom ◽  
B M Breckenridge ◽  
D J Wolff

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