Schistosomes express two forms of cathepsin D.
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.
Wong
J Y
JY
Queensland Institute of Medical Research, and Australian Centre for International and Tropical Health and Nutrition, Royal Brisbane Hospital, Herston.
Harrop
S A
SA
Day
S R
SR
Brindley
P J
PJ
D000595:Amino Acid Sequence; D000818:Animals; D015139:Blotting, Southern; D002402:Cathepsin D / Q000235:genetics*; D018076:DNA, Complementary / Q000235:genetics; D017238:Genes, Helminth; D006801:Humans; D008969:Molecular Sequence Data; D012550:Schistosoma mansoni / Q000201:enzymology*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D002402:Cathepsin D