ArticlePloS one2012
Simukunin from the salivary glands of the black fly Simulium vittatum inhibits enzymes that regulate clotting and inflammatory responses.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 53 citations in OpenAlex.
- Sialotranscriptome of Simulium pertinax and functional characterization of SpVaP: a novel recombinant simuliid-specific vasodilator.Molecular and cellular biochemistry · 2026Article
- The black fly salivary protein Simukunin inhibits complement activation through the lectin pathway protease MASP-2.The Journal of biological chemistry · 2026Article
- Bannakunin: a dual-target Kunitz inhibitor bridging anticoagulation (FXa/XIIa) and anti-platelet (α2β1/P2Y12) pathways.Cellular & molecular biology letters · 2026Article
- Dual-action salivary peptide drives black fly feeding efficiency.Communications biology · 2025Article
- Transcriptional phenotype of the anti-parasitic benzodiazepine meclonazepam on the blood fluke Schistosoma mansoni.PLoS neglected tropical diseases · 2025Article
- Guianensin, a Blackfly Salivary Protein, Inhibits the Lectin Pathway of Complement.Journal of medicinal chemistry · 2025Article
- Transcriptional phenotype of the anti-parasitic benzodiazepine meclonazepam on the blood flukebioRxiv : the preprint server for biology · 2024Article
- Article
- Platelet tissue factor pathway inhibitor-α dampens cardiac thrombosis and associated fibrosis in mice.Journal of thrombosis and haemostasis : JTH · 2023Article
- Proteomic analyses of venom from a Spider Hawk,The journal of venomous animals and toxins including tropical diseases · 2023Article
- Guianensin, aFrontiers in immunology · 2023Article
- Risk of Attacks by Blackflies (Diptera: Simuliidae) and Occurrence of Severe Skin Symptoms in Bitten Patients along the Eastern Border of the European Union.International journal of environmental research and public health · 2022Article
- Regulation of coagulation by tissue factor pathway inhibitor: Implications for hemophilia therapy.Journal of thrombosis and haemostasis : JTH · 2022Review
- Article
- KPI5 Is Involved in the Regulation of the Expression of Antibacterial Peptide Genes and Hemolymph Melanization in the Silkworm,Frontiers in immunology · 2022Article
- WPK5, a Novel Kunitz-Type Peptide from the LeechBiomedicines · 2021Article
- Schistosoma mansoni alter transcription of immunomodulatory gene products following in vivo praziquantel exposure.PLoS neglected tropical diseases · 2021Article
- Skin Lesions and Systemic Reactions in Humans Infested by Blackflies (Diptera: Simullidae) in Recreational Areas in Southeastern Poland.Journal of clinical medicine · 2021Article
- Identification, Characterization and Synthesis of Walterospermin, a Sperm Motility Activator from the Egyptian Black SnakeInternational journal of molecular sciences · 2020Article
- Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundBlack flies (Diptera: Simuliidae) feed on blood, and are important vectors of Onchocerca volvulus, the etiolytic agent of River Blindness. Blood feeding depends on pharmacological properties of saliva, including anticoagulation, but the molecules responsible for this activity have not been well characterized. METHODOLOGY/PRINCIPAL
findingsTwo Kunitz family proteins, SV-66 and SV-170, were identified in the sialome of the black fly Simulium vittatum. As Kunitz proteins are inhibitors of serine proteases, we hypothesized that SV-66 and/or -170 were involved in the anticoagulant activity of black fly saliva. Our results indicated that recombinant (r) SV-66 but not rSV-170 inhibited plasma coagulation. Mutational analysis suggested that SV-66 is a canonical BPTI-like inhibitor. Functional assays indicated that rSV66 reduced the activity of ten serine proteases, including several involved in mammalian coagulation. rSV-66 most strongly inhibited the activity of Factor Xa, elastase, and cathepsin G, exhibited lesser inhibitory activity against Factor IXa, Factor XIa, and plasmin, and exhibited no activity against Factor XIIa and thrombin. Surface plasmon resonance studies indicated that rSV-66 bound with highest affinity to elastase (K(D) = 0.4 nM) and to the active site of FXa (K(D) = 3.07 nM). We propose the name "Simukunin" for this novel protein.
conclusionsWe conclude that Simukunin preferentially inhibits Factor Xa. The inhibition of elastase and cathepsin G further suggests this protein may modulate inflammation, which could potentially affect pathogen transmission.
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