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

Mol Biochem Parasitol. 1989 Mar 1;33(2):113-22. doi: 10.1016/0166-6851(89)90025-x.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens, Helminth / biosynthesis
  • Antigens, Helminth / genetics*
  • Cathepsin B / genetics*
  • Cloning, Molecular
  • Cysteine Endopeptidases / genetics*
  • Helminth Proteins*
  • Humans
  • Immunoblotting
  • Mice
  • Molecular Sequence Data
  • Precipitin Tests
  • Protein Biosynthesis
  • Rats
  • Restriction Mapping
  • Schistosoma mansoni / enzymology
  • Schistosoma mansoni / genetics*
  • Schistosoma mansoni / immunology

Substances

  • Antigens, Helminth
  • Helminth Proteins
  • Cysteine Endopeptidases
  • Sm31 protein, Schistosoma mansoni
  • Cathepsin B

Associated data

  • GENBANK/J03984
  • GENBANK/M21308
  • GENBANK/M21309