M. Finken et al., CHARACTERIZATION OF THE COMPLETE PROTEIN DISULFIDE-ISOMERASE GENE OF SCHISTOSOMA-MANSONI AND IDENTIFICATION OF THE TISSUES OF ITS EXPRESSION, Molecular and biochemical parasitology, 64(1), 1994, pp. 135-144
cDNA and genomic clones of Schistosoma mansoni containing the complete
sequence of a homolog of protein disulfide isomerase have been identi
fied. The protein disulfide isomerase gene in schistosomes is a single
copy gene having a genomic structure that is very similar to that of
man. The C-terminus of the deduced protein is KDEL which in mammals fu
nctions as a signal sequence for retention of luminal proteins in the
endoplasmic reticulum. Immunohistology and in situ hybridization ident
ify the gastrodermis of the gut, the wall cells of the protonephridia,
and the sustentacular cells of the testes to be the major tissues of
protein disulfide isomerase gene expression. The protein disulfide iso
merase of schistosomes, produced in an expression vector in Escherichi
a coli, catalyzes disulfide/sulfhydryl isomerization in vitro.