ArticlePLoS neglected tropical diseases2014
Simplagrin, a platelet aggregation inhibitor from Simulium nigrimanum salivary glands specifically binds to the Von Willebrand factor receptor in collagen and inhibits carotid thrombus formation in vivo.
Article in PLoS neglected tropical diseases, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
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- Guianensin, a Blackfly Salivary Protein, Inhibits the Lectin Pathway of Complement.Journal of medicinal chemistry · 2025Article
- A deeper insight into the sialome of male and female Culex quinquefasciatus mosquitoes.BMC genomics · 2023Article
- Guianensin, aFrontiers in immunology · 2023Article
- Alboserpin, the Main Salivary Anticoagulant from the Disease VectorImmunoHorizons · 2022Article
- Biochemical characterization of AeD7L2 and its physiological relevance in blood feeding in the dengue mosquito vector, Aedes aegypti.The FEBS journal · 2021Article
- ADP binding by the Culex quinquefasciatus mosquito D7 salivary protein enhances blood feeding on mammals.Nature communications · 2020Article
- Anti-Thrombotic, Anti-Oxidant and Haemolysis Activities of Six Edible Insect Species.Foods (Basel, Switzerland) · 2020Article
- An insight into the sialotranscriptome and virome of Amazonian anophelines.BMC genomics · 2019Article
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Authors and funding
10 authors at 5 institutions in 2 countries.
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Abstract
backgroundAmong the several challenges faced by bloodsucking arthropods, the vertebrate hemostatic response against blood loss represents an important barrier to efficient blood feeding. Here we report the first inhibitor of collagen-induced platelet aggregation derived from the salivary glands of a black fly (Simulium nigrimanum), named Simplagrin. METHODS AND
findingsSimplagrin was expressed in mammalian cells and purified by affinity-and size-exclusion chromatography. Light-scattering studies showed that Simplagrin has an elongated monomeric form with a hydrodynamic radius of 5.6 nm. Simplagrin binds to collagen (type I-VI) with high affinity (2-15 nM), and this interaction does not involve any significant conformational change as determined by circular dichroism spectroscopy. Simplagrin-collagen interaction is both entropically and enthalpically driven with a large negative ΔG, indicating that this interaction is favorable and occurs spontaneously. Simplagrin specifically inhibits von Willebrand factor interaction with collagen type III and completely blocks platelet adhesion to collagen under flow conditions at high shear rates; however, Simplagrin failed to block glycoprotein VI and Iα2β1 interaction to collagen. Simplagrin binds to RGQOGVMGF peptide with an affinity (K(D) 11 nM) similar to that of Simplagrin for collagen. Furthermore, Simplagrin prevents laser-induced carotid thrombus formation in vivo without significant bleeding in mice and could be useful as an antithrombotic agent in thrombosis related disease.
conclusionOur results support the orthology of the Aegyptin clade in bloodsucking Nematocera and the hypothesis of a faster evolutionary rate of salivary function of proteins from blood feeding arthropods.
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