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.
Hamdan
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Institute of Parasitology, McGill University, Quebec, Canada.
Ribeiro
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary; D018509:DNA, Helminth; D017238:Genes, Helminth; D006801:Humans; D008245:Lysophospholipase / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D012550:Schistosoma mansoni / Q000201:enzymology* / Q000235:genetics / Q000302:isolation & purification; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA
D018076:DNA, Complementary; D018509:DNA, Helminth; D008245:Lysophospholipase