Jym. Wong et al., SCHISTOSOMES EXPRESS 2 FORMS OF CATHEPSIN-D, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1338(2), 1997, pp. 156-160
We report here a cDNA and its deduced amino acid sequence encoding a c
athepsin D-like, aspartic protease expressed by adult stages of the hu
man blood fluke Schistosoma mansoni. The cDNA encodes a short signal p
eptide, a pro-enzyme peptide of 37 amino acid residues, and a mature e
nzyme of 377 residues which has strong homology with mammalian catheps
ins D. This aspartic protease, although 84% identical in amino acids o
f the mature enzyme region to the previously reported cathepsin D from
the Asian schistosome S. japonicum, differs remarkably from the S. ja
ponicum enzyme in having a carboxyl terminal extension of 43 amino aci
d residues. These cathepsins D of schistosomes may play pivotal roles
in the degradation of hemoglobin obtained by the parasites from ingest
ed host erythrocytes. (C) 1997 Elsevier Science B.V.