Abstract
We report here a cDNA and its deduced amino acid sequence encoding a cathepsin D-like, aspartic protease expressed by adult stages of the human blood fluke Schistosoma mansoni. The cDNA encodes a short signal peptide, a pro-enzyme peptide of 37 amino acid residues, and a mature enzyme of 377 residues which has strong homology with mammalian cathepsins D. This aspartic protease, although 84% identical in amino acids of the mature enzyme region to the previously reported cathepsin D from the Asian schistosome S. japonicum, differs remarkably from the S. japonicum enzyme in having a carboxyl terminal extension of 43 amino acid residues. These cathepsins D of schistosomes may play pivotal roles in the degradation of hemoglobin obtained by the parasites from ingested host erythrocytes. © 1997 Elsevier Science B.V. All rights reserved.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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