ArticleThe Journal of biological chemistry2020
Structural characterization of anti-CCL5 activity of the tick salivary protein evasin-4.
Article in The Journal of biological chemistry, 2020. 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, 16 citations in OpenAlex.
- Evasins: Biology and Therapeutic Potential of Broad-Spectrum Chemokine Inhibitors.Basic & clinical pharmacology & toxicology · 2026Review
- Chemokine-Binding All-D-CLIPS Peptides Identified Using Mirror-Image Phage Display.ACS chemical biology · 2025Article
- Filamentous chemokine CCL5 structure and the functional aspects.Scientific reports · 2025Article
- Structural basis of chemokine recognition by the class A3 tick evasin EVA-ACA1001.Protein science : a publication of the Protein Society · 2024Article
- Discovery and pharmacophoric characterization of chemokine network inhibitors using phage-display, saturation mutagenesis and computational modelling.Nature communications · 2023Article
- A Deeper Insight into the Tick Salivary Protein Families under the Light of Alphafold2 and Dali: Introducing the TickSialoFam 2.0 Database.International journal of molecular sciences · 2022Article
- Structure-guided engineering of tick evasins for targeting chemokines in inflammatory diseases.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Combined Antiplatelet Therapy Reduces the Proinflammatory Properties of Activated Platelets.TH open : companion journal to thrombosis and haemostasis · 2021Article
- A Cornflower Extract ContainingMediators of inflammation · 2021Article
- Anti-inflammatory activities of arthropod peptides: a systematic review.The journal of venomous animals and toxins including tropical diseases · 2021Review
- Phylogenetic Analysis Indicates That Evasin-Like Proteins of Ixodid Ticks Fall Into Three Distinct Classes.Frontiers in cellular and infection microbiology · 2021Article
- Immunomodulatory Proteins in Tick Saliva From a Structural Perspective.Frontiers in cellular and infection microbiology · 2021Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ticks, as blood-sucking parasites, have developed a complex strategy to evade and suppress host immune responses during feeding. The crucial part of this strategy is expression of a broad family of salivary proteins, called Evasins, to neutralize chemokines responsible for cell trafficking and recruitment. However, structural information about Evasins is still scarce, and little is known about the structural determinants of their binding mechanism to chemokines. Here, we studied the structurally uncharacterized Evasin-4, which neutralizes a broad range of CC-motif chemokines, including the chemokine CC-motif ligand 5 (CCL5) involved in atherogenesis. Crystal structures of Evasin-4 and E66S CCL5, an obligatory dimeric variant of CCL5, were determined to a resolution of 1.3-1.8 Å. The Evasin-4 crystal structure revealed an L-shaped architecture formed by an N- and C-terminal subdomain consisting of eight β-strands and an α-helix that adopts a substantially different position compared with closely related Evasin-1. Further investigation into E66S CCL5-Evasin-4 complex formation with NMR spectroscopy showed that residues of the N terminus are involved in binding to CCL5. The peptide derived from the N-terminal region of Evasin-4 possessed nanomolar affinity to CCL5 and inhibited CCL5 activity in monocyte migration assays. This suggests that Evasin-4 derivatives could be used as a starting point for the development of anti-inflammatory drugs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.