Cloning and sequence analysis of a lysophospholipase homologue from Schistosoma mansoni

A novel cDNA encoding a lysophospholipase (SmLPLH) homologue has been cloned from the human parasite, Schistosoma mansoni. The predicted primary structure of SmLPLH shares high sequence homology with mammalian lysophospholipases (62%) and also contains aconsensus signature peptide (GXSXG), which is present in all lipases. Two splice variants of SmLPLH that differ by 32 N-terminal amino acids were identified. The shorter truncated species carries a conserved S. mansoni spliced leader (SL) sequence at its 5' end and is believed to be formed by trans-splicing of the SL to an internal exon splice site. The functional significance of these two isoforms of SmLPLH is currently unknown.