In silico analysis of molecular mimicry between human aquaporin 3, Aspergillus fumigatus aquaporin and aquaporins from allergic sources.

Autor: Andres Sanchez, Yaquelin Padilla, Adriana Lorduy, Jorge Sanchez, Marlon Munera, Claudia Baena, Carlos Bernal, Juan Urrego
Jazyk: English<br />Spanish; Castilian
Rok vydání: 2024
Předmět:
Zdroj: Revista Alergia México, Vol 71, Iss 1 (2024)
Druh dokumentu: article
ISSN: 0002-5151
2448-9190
DOI: 10.29262/ram.v71i1.1370
Popis: Background: Atopic dermatitis (AD) profoundly impacts quality of life as a chronic inflammatory skin disease. Allergen exposure triggers specific IgE antibodies, initiating allergy symptoms. Cross-reactivity, linked to auto-IgE responses, potentially influences AD severity. Exploring new allergens and self-autoantigens, like Aspergillus fumigatus, enhances knowledge of AD triggers. Our focus was on analyzing molecular mimicry between human AQP3 and A. fumigatus aquaporin, alongside various allergenic sources. Objective: Conduct an in silico assessment of potential molecular mimicry between human aquaporins, A. fumigatus, and diverse allergenic sources. Methods: Amino acid sequences of human AQP3 and A. fumigatus aquaporin were compared through multiple alignments with 25 aquaporins from diverse allergenic sources. Phylogenetic analysis and homology-based modeling were executed, and ElliPro server predicted conserved antigenic regions on 3D structures. Results: Global identity among studied aquaporins was 32.6%, with a specific conserved local region at 71.4%. Five monophyletic clades (A-E) were formed, and Group B displayed the highest identity (95%), including 6 mammalian aquaporins, notably AQP3. A. fumigatus aquaporin exhibited the highest identity with Malassezia sympodialis (35%). Three linear and three discontinuous epitopes were identified in both human and A. fumigatus aquaporins. The Root Mean Square Deviation (RMSD) from overlapping aquaporin structures was 1.006. Conclusion: Identification of potential linear and conformational epitopes on human AQP3 suggests likely molecular mimicry with A. fumigatus aquaporins. High identity in a specific antigenic region indicates potential autoreactivity and a probable antigenic site involved in cross-reactivity. Validation through in vitro and in vivo studies is essential for further understanding and confirmation.
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