ArticleThe Journal of biological chemistry2014
Identification of the pharmacophore of the CC chemokine-binding proteins Evasin-1 and -4 using phage display.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Evasins: Biology and Therapeutic Potential of Broad-Spectrum Chemokine Inhibitors.Basic & clinical pharmacology & toxicology · 2026Review
- Structural basis of chemokine recognition by the class A3 tick evasin EVA-ACA1001.Protein science : a publication of the Protein Society · 2024Article
- The binding and specificity of chemokine binding proteins, through the lens of experiment and computation.Biomedical journal · 2022Review
- 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
- Perspectives on the Biological Role of Chemokine:Glycosaminoglycan Interactions.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2021Review
- Structural characterization of anti-CCL5 activity of the tick salivary protein evasin-4.The Journal of biological chemistry · 2020Article
- Understanding the mechanisms that facilitate specificity, not redundancy, of chemokine-mediated leukocyte recruitment.Immunology · 2020Review
- Evasins: Tick Salivary Proteins that Inhibit Mammalian Chemokines.Trends in biochemical sciences · 2020Review
- Tick saliva protein Evasin-3 modulates chemotaxis by disrupting CXCL8 interactions with glycosaminoglycans and CXCR2.The Journal of biological chemistry · 2019Article
- The N-terminal domain of a tick evasin is critical for chemokine binding and neutralization and confers specific binding activity to other evasins.The Journal of biological chemistry · 2018Article
- Evasin-displaying lactic acid bacteria bind different chemokines and neutralize CXCL8 production in Caco-2 cells.Microbial biotechnology · 2017Article
- Chemokines from a Structural Perspective.International journal of molecular sciences · 2017Review
- Ticks from diverse genera encode chemokine-inhibitory evasin proteins.The Journal of biological chemistry · 2017Article
- Yeast surface display identifies a family of evasins from ticks with novel polyvalent CC chemokine-binding activities.Scientific reports · 2017Article
- Evasins: Therapeutic Potential of a New Family of Chemokine-Binding Proteins from Ticks.Frontiers in immunology · 2016Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
To elucidate the ligand-binding surface of the CC chemokine-binding proteins Evasin-1 and Evasin-4, produced by the tick Rhipicephalus sanguineus, we sought to identify the key determinants responsible for their different chemokine selectivities by expressing Evasin mutants using phage display. We first designed alanine mutants based on the Evasin-1·CCL3 complex structure and an in silico model of Evasin-4 bound to CCL3. The mutants were displayed on M13 phage particles, and binding to chemokine was assessed by ELISA. Selected variants were then produced as purified proteins and characterized by surface plasmon resonance analysis and inhibition of chemotaxis. The method was validated by confirming the importance of Phe-14 and Trp-89 to the inhibitory properties of Evasin-1 and led to the identification of a third crucial residue, Asn-88. Two amino acids, Glu-16 and Tyr-19, were identified as key residues for binding and inhibition of Evasin-4. In a parallel approach, we identified one clone (Y28Q/N60D) that showed a clear reduction in binding to CCL3, CCL5, and CCL8. It therefore appears that Evasin-1 and -4 use different pharmacophores to bind CC chemokines, with the principal binding occurring through the C terminus of Evasin-1, but through the N-terminal region of Evasin-4. However, both proteins appear to target chemokine N termini, presumably because these domains are key to receptor signaling. The results also suggest that phage display may offer a useful approach for rapid investigation of the pharmacophores of small inhibitory binding proteins.
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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.