Lysophospholipase from the human blood fluke, Schistosoma japonicum

Fan, Jinjiang, Yang, Wen and Brindley, Paul J. (2008) Lysophospholipase from the human blood fluke, Schistosoma japonicum. International Journal of Infectious Diseases, 12 2: 143-151. doi:10.1016/j.ijid.2007.05.005

Author Fan, Jinjiang
Yang, Wen
Brindley, Paul J.
Title Lysophospholipase from the human blood fluke, Schistosoma japonicum
Formatted title
Lysophospholipase from the human blood fluke, Schistosoma japonicum
Journal name International Journal of Infectious Diseases   Check publisher's open access policy
ISSN 1201-9712
Publication date 2008-03-01
Year available 2007
Sub-type Article (original research)
DOI 10.1016/j.ijid.2007.05.005
Open Access Status DOI
Volume 12
Issue 2
Start page 143
End page 151
Total pages 9
Place of publication Oxford, MA, United Kingdom
Publisher Elsevier
Language eng
Formatted abstract
Background: Given the unusual nature of the schistosome surface (a highly unusual lipid bi-layer) and the central role of the schistosome tegument in host–parasite relations, an enhanced understanding of the lipid biochemistry of the schistosome surface can be expected to provide new insights into schistosome pathogenesis and lead to new interventions.
Methods: Bioinformatics approaches including three-dimensional homology modeling, along with recombinant expression, dimensional gel electrophoresis, immunoblotting, and Southern hybridizations were employed to characterize a novel lysophospholipase gene transcript from Schistosoma japonicum.
Results: A transcript encoding a small form lysophospholipase from the egg stage of S. japonicum was isolated as an expressed sequence tag (EST). The deduced polypeptide included 227 amino acid residues, shared identity with lysophospholipases of Schistosoma mansoni and Rattus norvegicus, and esterase A of Pseudomonas fluorescens, appeared to belong to the abhydrolase_2 family of phospholipases and carboxylesterases, and was structurally related to the α/β-hydrolases (pfam00561). The S. japonicum enzyme exhibited the GXSXG consensus active site characteristic of serine proteases, esterases, and lipases, and included the catalytic triad motif of Ser–Asp–His residues characteristic of serine hydrolases. Three-dimensional structural predictions accomplished using the coordinates of human acyl protein thioesterase and P. fluorescens esterase indicated that the putative catalytic triad formed by these three residues was located at the α/β-hydrolase fold characteristic of the lipases and esterases. Soluble S. japonicum lysophospholipase was expressed in Escherichia coli as a recombinant enzyme of ∼26 kDa and employed to raise a mono-specific antiserum. Immunoblot analysis revealed a single 23-kDa band in both membrane-associated and soluble tissue fractions of adult schistosomes. Southern hybridization and bioinformatics analyses indicated the likely presence of allelic-specific polymorphisms and/or two copies of the lysophospholipase gene in the S. japonicum genome.
Conclusions: A small form lysophospholipase has been characterized from the human schistosome, S. japonicum. The availability of the recombinant S. japonicum lysophospholipase should facilitate further characterization of the enzyme, including its substrate and inhibition profiles and its potential as an interventional target. Schistosome lysophospholipase may represent a new target for anti-schistosomal chemotherapy given that metrifonate, which targets the related enzyme acetylcholinesterase, is an effective and safe medicine for treatment of urinary schistosomiasis.
Keyword Schistosome
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ
Additional Notes Available online 20 August 2007

Document type: Journal Article
Sub-type: Article (original research)
Collection: Australian Centre for International & Tropical Health
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Created: Thu, 03 Sep 2009, 20:22:50 EST by Mr Andrew Martlew on behalf of Australian Centre for International and Tropical Health and Nutrition