ArticlePLoS neglected tropical diseases2018
SmSP2: A serine protease secreted by the blood fluke pathogen Schistosoma mansoni with anti-hemostatic properties.
Article in PLoS neglected tropical diseases, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 53 citations in OpenAlex.
- Fibrinolysis-unrelated functions of the plasminogen/plasmin system: A gateway to successful parasitism?Current research in parasitology & vector-borne diseases · 2026Review
- Transcriptomics analysis of in vivo Opisthorchis viverrini: Stage-specific gene expression and novel genes with stable expression in mammalian stages for opisthorchiasis intervention.PLoS neglected tropical diseases · 2025Article
- A genome-scale drug discovery pipeline uncovers new therapeutic targets and a unique p97 allosteric binding site inbioRxiv : the preprint server for biology · 2025Article
- Binding and cleavage of pro-urokinase by a tegument extract of Fasciola hepatica newly excysted juveniles activate the host fibrinolytic system.Veterinary research · 2025Article
- An overview of qualitative and quantitative platelet abnormalities in schistosomiasis.Parasitology research · 2024Review
- A cercarial invadolysin interferes with the host immune response and facilitates infection establishment of Schistosoma mansoni.PLoS pathogens · 2023Article
- Hidden in plain sight: How helminths manage to thrive in host blood.Frontiers in parasitology · 2023Review
- Discovery of new Schistosoma mansoni aspartyl protease inhibitors by structure-based virtual screening.Memorias do Instituto Oswaldo Cruz · 2023Article
- Multiplex substrate profiling by mass spectrometry for proteases.Methods in enzymology · 2023Article
- Characterization of glutamate carboxypeptidase 2 orthologs in trematodes.Parasites & vectors · 2022Article
- Novel Inhibitors and Activity-Based Probes Targeting Trypsin-Like Serine Proteases.Frontiers in chemistry · 2022Article
- Novel inhibitors and activity-based probes targeting serine proteases.Frontiers in chemistry · 2022Article
- Article
- Selective Neutral pH Inhibitor of Cathepsin B Designed Based on Cleavage Preferences at Cytosolic and Lysosomal pH Conditions.ACS chemical biology · 2021Article
- Spatial expression pattern of serine proteases in the blood fluke Schistosoma mansoni determined by fluorescence RNA in situ hybridization.Parasites & vectors · 2021Article
- Review
- Kinins and Their Receptors in Infectious Diseases.Pharmaceuticals (Basel, Switzerland) · 2020Review
- Serum amyloid A is a soluble pattern recognition receptor that drives type 2 immunity.Nature immunology · 2020Article
- Article
- Immune Evasion Strategies of Schistosomes.Frontiers in immunology · 2020Review
Corrections and comments
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Authors and funding
14 authors at 5 institutions in 2 countries.
Funding
Abstract
backgroundSerine proteases are important virulence factors for many pathogens. Recently, we discovered a group of trypsin-like serine proteases with domain organization unique to flatworm parasites and containing a thrombospondin type 1 repeat (TSR-1). These proteases are recognized as antigens during host infection and may prove useful as anthelminthic vaccines, however their molecular characteristics are under-studied. Here, we characterize the structural and proteolytic attributes of serine protease 2 (SmSP2) from Schistosoma mansoni, one of the major species responsible for the tropical infectious disease, schistosomiasis. METHODOLOGY/PRINCIPAL
findingsSmSP2 comprises three domains: a histidine stretch, TSR-1 and a serine protease domain. The cleavage specificity of recombinant SmSP2 was determined using positional scanning and multiplex combinatorial libraries and the determinants of specificity were identified with 3D homology models, demonstrating a trypsin-like endopeptidase mode of action. SmSP2 displayed restricted proteolysis on protein substrates. It activated tissue plasminogen activator and plasminogen as key components of the fibrinolytic system, and released the vasoregulatory peptide, kinin, from kininogen. SmSP2 was detected in the surface tegument, esophageal glands and reproductive organs of the adult parasite by immunofluorescence microscopy, and in the excretory/secretory products by immunoblotting. CONCLUSIONS/SIGNIFICANCE: The data suggest that SmSP2 is secreted, functions at the host-parasite interface and contributes to the survival of the parasite by manipulating host vasodilatation and fibrinolysis. SmSP2 may be, therefore, a potential target for anti-schistosomal therapy.
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