ArticleInternational journal for parasitology2009
Schistosoma mansoni arginase shares functional similarities with human orthologs but depends upon disulphide bridges for enzymatic activity.
Article in International journal for parasitology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- The arginase-polyamine signaling axis in immune cells: Implications for immune modulation and host-pathogen interactions.iScience · 2026Review
- Transcriptome of the parasitic flatworm Schistosoma mansoni during intra-mammalian development.PLoS neglected tropical diseases · 2020Article
- Combining bioinformatics, cheminformatics, functional genomics and whole organism approaches for identifying epigenetic drug targets in Schistosoma mansoni.International journal for parasitology. Drugs and drug resistance · 2018Article
- Crystal structure of Schistosoma mansoni arginase, a potential drug target for the treatment of schistosomiasis.Biochemistry · 2014Article
- Unique T cells with unconventional cytokine profiles induced in the livers of mice during Schistosoma mansoni infection.PloS one · 2013Article
- Unique hepatic cytosolic arginase evolved independently in ureogenic freshwater air-breathing teleost, Heteropneustes fossilis.PloS one · 2013Article
- Modulation of the arginase pathway in the context of microbial pathogenesis: a metabolic enzyme moonlighting as an immune modulator.PLoS pathogens · 2010Review
- Anti-schistosomal intervention targets identified by lifecycle transcriptomic analyses.PLoS neglected tropical diseases · 2009Article
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Authors and funding
7 authors at 4 institutions in 4 countries.
Funding
Abstract
Schistosome helminths constitute a major health risk for the human population in many tropical areas. We demonstrate for the first time that several developmental stages of the human parasite Schistosoma mansoni express arginase, which is responsible for the hydrolysis of l-arginine to l-ornithine and urea. Arginase activity by alternatively activated macrophages is an essential component of the mammalian host response in schistosomiasis. However, it has not been previously shown that the parasite also expresses arginase when it is in contact with the mammalian host. After cloning and sequencing the cDNA encoding the parasite enzyme, we found that many structural features of human arginase are well conserved in the parasite ortholog. Subsequently, we discovered that S. mansoni arginase shares many similar molecular, biochemical and functional properties with both human arginase isoforms. Nevertheless, our data also reveal striking differences between human and schistosome arginase. Particularly, we found evidence that schistosome arginase activity depends upon disulphide bonds by cysteines, in contrast to human arginase. In conclusion, we report that S. mansoni arginase is well adapted to the physiological conditions that exist in the human host.
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