Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Bioinformatics Study on Site-Specific Variations of Eotaxin-3, a Key Chemokine in Eosinophilic Esophagitis (EoE)

Version 1 : Received: 9 July 2024 / Approved: 10 July 2024 / Online: 10 July 2024 (14:07:18 CEST)

How to cite: Giordano, D.; D’Acierno, A.; Marabotti, A.; Iovino, P.; Iacomino, G.; Facchiano, A. Bioinformatics Study on Site-Specific Variations of Eotaxin-3, a Key Chemokine in Eosinophilic Esophagitis (EoE). Preprints 2024, 2024070870. https://doi.org/10.20944/preprints202407.0870.v1 Giordano, D.; D’Acierno, A.; Marabotti, A.; Iovino, P.; Iacomino, G.; Facchiano, A. Bioinformatics Study on Site-Specific Variations of Eotaxin-3, a Key Chemokine in Eosinophilic Esophagitis (EoE). Preprints 2024, 2024070870. https://doi.org/10.20944/preprints202407.0870.v1

Abstract

Eotaxin-3 is a key chemokine with a relevant role in eosinophilic esophagitis, a rare chronic immune/antigen-mediated inflammatory disorder. Eotaxin-3 is a potent activator of eosinophil emergence and migration, which may lead to allergic airway inflammation. We investigated by bioinformatics tools the protein structure and the possible effects of the known variations reported in public databases. Following a procedure already established, we created a 3D model of the whole protein and modelled the structure of 105 protein variants due to known point mutations. The effects of the amino acid substitution at the level of impact on protein structure, stability, and possibly function, were detected by the bioinformatics procedure and described in detail. A web application was implemented to browse the results of the analysis and visualize the 3D models, with the opportunity of downloading the models and analyze by the own software. Among 105 amino acid substitutions investigated, the study evidenced in 44 cases at least one change in any of the investigated structural parameters. Other 6 variations are also relevant, although a structural effect is not detected by our analysis, because they substituted amino acids highly conserved, which suggests a possible function role. All these variations should be the object of particular attention, as they may induce loss of functionality in the protein.

Keywords

eosinophilic esophagitis; protein variants; protein structural analysis; protein modelling; web application

Subject

Biology and Life Sciences, Biochemistry and Molecular Biology

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