ArticleScientific reports2023
Development of an inhibiting antibody against equine interleukin 5 to treat insect bite hypersensitivity of horses.
Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Phage Display Derived Antibodies Against Antimicrobial Peptide FsPDF2 Reveal Stress Response in European Beech.Plant biotechnology journal · 2026Article
- A Comparative Review of Cytokines and Cytokine Targeting in Sepsis: From Humans to Horses.Cells · 2024Review
- Using high-density SNP data to unravel the origin of the Franches-Montagnes horse breed.Genetics, selection, evolution : GSE · 2024Article
- Human antibodies neutralizing the alpha-latrotoxin of the European black widow.Frontiers in immunology · 2024Article
- Insect Bite Hypersensitivity in Horses: Causes, Diagnosis, Scoring and New Therapies.Animals : an open access journal from MDPI · 2023Review
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Insect bite hypersensitivity (IBH) is the most common allergic skin disease of horses. It is caused by insect bites of the Culicoides spp. which mediate a type I/IVb allergy with strong involvement of eosinophil cells. No specific treatment option is available so far. One concept could be the use of a therapeutic antibody targeting equine interleukin 5, the main activator and regulator of eosinophils. Therefore, antibodies were selected by phage display using the naïve human antibody gene libraries HAL9/10, tested in a cellular in vitro inhibition assay and subjected to an in vitro affinity maturation. In total, 28 antibodies were selected by phage display out of which eleven have been found to be inhibiting in the final format as chimeric immunoglobulin G with equine constant domains. The two most promising candidates were further improved by in vitro affinity maturation up to factor 2.5 regarding their binding activity and up to factor 2.0 regarding their inhibition effect. The final antibody named NOL226-2-D10 showed a strong inhibition of the interleukin 5 binding to its receptor (IC
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