Exploring the repertoire of cross-reactive allergens among Aspergillus fumigatus and D. pteronyssinus mites: an in-silico approach.

Saved in:
Bibliographic Details
Title: Exploring the repertoire of cross-reactive allergens among Aspergillus fumigatus and D. pteronyssinus mites: an in-silico approach.
Alternate Title: Exploración de los alérgenos de reactividad cruzada entre los ácaros Aspergillus fumigatus y D. pteronyssinus: un enfoque in silico.
Authors: Vasquez, José J.1, Sanchez, Andrés2,3, Sancez, Jorge3, García, Elizabeth2, Múnera, Marlon2,4 marmunera@gmail.com
Source: Revista Alergia de Mexico. oct-dic2025, Vol. 72 Issue 4, p281-289. 9p.
Subjects: ASPERGILLUS fumigatus, DERMATOPHAGOIDES pteronyssinus, BIOINFORMATICS, ALLERGENS, ALLERGIES, B cells
Abstract (English): Objective: To examinate the potential cross reactivity among A. fumigatus and mites, both important allergenic source in tropical regions, using mainly a bioinformatic approach. Methods: Amino acid sequences from allergens from Aspergillus fumigatus reported in the allergome database were retrieved and used as input to perform PSI-BLAST against Dermatophagoides pteronyssinus's proteome. Results with similitudes and query cover values above 25% and 80%, respectively, were selected to further analysis. B cell epitope prediction was done by using the Ellipro tool. Just epitopes conserved between both allergenic sources were informed and displayed on 3D model surfaces obtained by modeling based on homology. Results: Twelve allergens from Aspergillus fumigatus shared homology with proteins reported in D. pteronyssinus. All 3D models obtained showed typical folding to the protein family they belonged. Ribosomal protein L3, Molecular chaperone Mod-E/Hsp90, Acidic ribosomal protein P2, Enolase, and peptidyl-propyl cis-trans isomerase were allergens with the highest identity score (>60%). At least four B linear epitopes were predicted to be shared between allergens and homologous in D. pteronyssinus. Conclusion: Results indicated that cross-reactivity between Aspergillus fumigatus and D. pteronyssinus is feasible. At least twelve allergens could be involved, and this could explain how molds increase sensitization to mites. In vitro analyses are needed to confirm these results. [ABSTRACT FROM AUTHOR]
Abstract (Spanish): Objetivo: Examinar la posible reactividad cruzada entre A. fumigatus y los ácaros, ambas importantes fuentes de alérgenos en regiones tropicales, mediante un enfoque bioinformático. Métodos: Se recuperaron las secuencias de aminoácidos de alérgenos de Aspergillus fumigatus registradas en la base de datos del alergoma y se utilizaron como entrada para realizar un análisis PSI-BLAST contra el proteoma de Dermatophagoides pteronyssinus. Se seleccionaron para su posterior análisis los resultados con similitudes y valores de cobertura de consulta superiores al 25 y al 80%, respectivamente. La predicción de epítopos de células B se realizó mediante la herramienta Ellipro. Solo se identificaron los epítopos conservados entre ambas fuentes alergénicas y se visualizaron en superficies de modelos 3D obtenidas mediante modelado basado en homología. Resultados: Doce alérgenos de Aspergillus fumigatus compartieron homología con proteínas descritas en D. pteronyssinus. Todos los modelos 3D obtenidos mostraron el plegamiento típico de la familia proteica a la que pertenecen. La proteína ribosomal L3, la chaperona molecular Mod-E/Hsp90, la proteína ribosomal ácida P2, la enolasa y la peptidil-propil cis-trans-isomerasa fueron los alérgenos con mayor puntuación de identidad (>60%). Se predijo que al menos cuatro epítopos lineales B eran compartidos entre los alérgenos y homólogos en D. pteronyssinus. Conclusión: Los resultados indicaron que la reactividad cruzada entre Aspergillus fumigatus y D. pteronyssinus es factible. Al menos doce alérgenos pueden estar implicados, lo que explica cómo los mohos aumentan la sensibilización a los ácaros. Se requieren análisis in vitro para confirmar estos resultados. [ABSTRACT FROM AUTHOR]
Copyright of Revista Alergia de Mexico is the property of Coleg. Mexicano de Inmunologia Clinica y Alergia A.C.; Soc. Lat. de Alergia, Asma e Inmunologia and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: MedicLatina
Description
Abstract:Objective: To examinate the potential cross reactivity among A. fumigatus and mites, both important allergenic source in tropical regions, using mainly a bioinformatic approach. Methods: Amino acid sequences from allergens from Aspergillus fumigatus reported in the allergome database were retrieved and used as input to perform PSI-BLAST against Dermatophagoides pteronyssinus's proteome. Results with similitudes and query cover values above 25% and 80%, respectively, were selected to further analysis. B cell epitope prediction was done by using the Ellipro tool. Just epitopes conserved between both allergenic sources were informed and displayed on 3D model surfaces obtained by modeling based on homology. Results: Twelve allergens from Aspergillus fumigatus shared homology with proteins reported in D. pteronyssinus. All 3D models obtained showed typical folding to the protein family they belonged. Ribosomal protein L3, Molecular chaperone Mod-E/Hsp90, Acidic ribosomal protein P2, Enolase, and peptidyl-propyl cis-trans isomerase were allergens with the highest identity score (>60%). At least four B linear epitopes were predicted to be shared between allergens and homologous in D. pteronyssinus. Conclusion: Results indicated that cross-reactivity between Aspergillus fumigatus and D. pteronyssinus is feasible. At least twelve allergens could be involved, and this could explain how molds increase sensitization to mites. In vitro analyses are needed to confirm these results. [ABSTRACT FROM AUTHOR]
ISSN:00025151
DOI:10.29262/ram.v72i4.1414