ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Crystallization and diffraction analysis of the serpin IRS-2 from the hard tick Ixodes ricinus.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Conformational transition of the Ixodes ricinus salivary serpin Iripin-4.Acta crystallographica. Section D, Structural biology · 2023Article
- rDromaserpin: A Novel Anti-Hemostatic Serpin, from the Salivary Glands of the Hard TickToxins · 2021Article
- Structural and biochemical characterization of the novel serpin Iripin-5 from Ixodes ricinus.Acta crystallographica. Section D, Structural biology · 2021Article
- Article
- Iripin-3, a New Salivary Protein Isolated FromFrontiers in immunology · 2021Article
- Protease Inhibitors in Tick Saliva: The Role of Serpins and Cystatins in Tick-host-Pathogen Interaction.Frontiers in cellular and infection microbiology · 2017Review
- Ixodes scapularis Tick Saliva Proteins Sequentially Secreted Every 24 h during Blood Feeding.PLoS neglected tropical diseases · 2016Article
- Ixodes ricinus salivary serpin IRS-2 affects Th17 differentiation via inhibition of the interleukin-6/STAT-3 signaling pathway.Infection and immunity · 2015Article
- Rhipicephalus microplus serine protease inhibitor family: annotation, expression and functional characterisation assessment.Parasites & vectors · 2015Article
- A blood meal-induced Ixodes scapularis tick saliva serpin inhibits trypsin and thrombin, and interferes with platelet aggregation and blood clotting.International journal for parasitology · 2014Article
- Amblyomma americanum tick saliva serine protease inhibitor 6 is a cross-class inhibitor of serine proteases and papain-like cysteine proteases that delays plasma clotting and inhibits platelet aggregation.Insect molecular biology · 2013Article
- Article
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6 authors.
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Abstract
IRS-2 from the hard tick Ixodes ricinus belongs to the serpin family of protease inhibitors. It is produced in the salivary glands of the tick and its anti-inflammatory activity suggests that it plays a role in parasite-host interaction. Recombinant IRS-2 prepared by heterologous expression in a bacterial system was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to the primitive tetragonal space group P4(3) and diffracted to 1.8 Å resolution. Mass-spectrometric and electrophoretic analyses revealed that IRS-2 was cleaved by contaminating proteases during crystallization. This processing of IRS-2 mimicked the specific cleavage of the serpin by its target protease and resulted in a more stable form (the so-called relaxed conformation), which produced well diffracting crystals. Activity profiling with specific substrates and inhibitors demonstrated traces of serine and cysteine proteases in the protein stock solution.
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