Antioxidant enzymes are thought to play a crucial role in the survival
of the parasite, Schistosoma mansoni, during its migration through th
e tissues of the definitive host. We recently cloned the cDNA encoding
one such enzyme, glutathione peroxidase (Gpx). In order to elucidate
the regulation of expression of this gene, we describe the cloning and
characterization of a Gpx gene of S. mansoni. An initial screen of a
lambda EMBL4 genomic library using the corresponding cDNA sequence as
a probe yielded 14 positive clones, two of which have so far been anal
yzed in detail. The complete Gpx gene contains five introns, four of w
hich, located at the 5' end, are extremely short (30-51 bp) and the la
st of which is approximately 6 kb long. We present the sequence of the
gene including 73 bp at the 5' end, the complete sequence to 137 bp d
ownstream from the penultimate exon, 164 bp upstream and 131 bp downst
ream from the last 3' exon. The potential mRNA cap site is situated 21
9 bp upstream from the ATG start codon. All intron/exon junctions corr
espond to the conventional eukaryotic splice signal. Analysis of the 5
' flanking region revealed the presence of a potential TATA box at -26
bp from the cap site, but no CAAT-like element is present. Southern b
lot analysis showed a unique Gpx gene organisation in the S. mansoni g
enome.