Primary structures of Sm31/32 diagnostic proteins of Schistosoma mansoni and their identification as proteases

We have constructed cDNA clones containing the complete nucleotide sequences coding for two highly antigenic Schistosoma mansoni adult worm proteins, Sm31 and Sm32. The predicted amino acid sequence of Sm31 shows significant homology to mouse, rat and human cathepsin B. The nucleotide sequence of Sm...

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Veröffentlicht in:Molecular and biochemical parasitology 1989-03, Vol.33 (2), p.113-122
Hauptverfasser: Klinkert, Mo-Quen, Felleisen, Richard, Link, Gisela, Ruppel, Andreas, Beck, Ewald
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Sprache:eng
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Zusammenfassung:We have constructed cDNA clones containing the complete nucleotide sequences coding for two highly antigenic Schistosoma mansoni adult worm proteins, Sm31 and Sm32. The predicted amino acid sequence of Sm31 shows significant homology to mouse, rat and human cathepsin B. The nucleotide sequence of Sm32 is identical to that reported by others for S. mansoni ‘haemoglobinase’. The different nucleotide sequences demonstrate the existence of two different proteolytic enzymes, both of which are synthesised in the form of precursor molecules. Structural homology of the schistosome cathepsin B to the mammalian ones indicates that the mature protein is processed from a propeptide. The calculated molecular weight of haemoglobinase of 47 000 suggests that post-translational processing is also involved in generating an active protease.
ISSN:0166-6851
1872-9428
DOI:10.1016/0166-6851(89)90025-X