Toward Consensus Epitopes B and T of Tropomyosin Involved in Cross-Reactivity across Diverse Allergens: An In Silico Study

• Published in: Biomedicines Vol. 12; no. 4; p. 884
• Main Authors: Martínez, Dalgys, Fang, Luis, Meza-Torres, Catherine, Garavito, Gloria, López-Lluch, Guillermo, Egea, Eduardo
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01-04-2024
• Subjects: allergen; Allergens; Allergic diseases; Allergic reaction; Allergies; Allergy; Amino acids; Analysis; Antigenic determinants; B cells; B-cell epitope; Cluster analysis; Cockroaches; Cross-reactivity; Epitopes; IgE epitope; Immune response; Immunoglobulin E; Immunology; Immunotherapy; Informatics; Ligands; Lymphocytes; Lymphocytes B; Lymphocytes T; Major histocompatibility complex; Muscle proteins; Peptides; Phylogenetics; Proteins; Shellfish; T cells; T-cell epitope; Tropical environment; Tropomyosin; IgE epitope; allergen; cross-reactivity; tropomyosin; B-cell epitope; T-cell epitope
• ISSN: 2227-9059; 2227-9059
• DOI: 10.3390/biomedicines12040884

Tropomyosin (TM) is a pan-allergen with cross-reactivity to arthropods, insects, and nematodes in tropical regions. While IgE epitopes of TM contribute to sensitization, T-cell (MHC-II) epitopes polarize the Th2 immune response. This study aimed to identify linear B and T consensus epitopes among house dust mites, cockroaches,
, shrimp, and mosquitoes, exploring the molecular basis of cross-reactivity in allergic diseases. Amino acid sequences of Der p 10, Der f 10, Blo t 10, Lit v 1, Pen a 1, Pen m 1, rAsc l 3, Per a 7, Bla g 7, and Aed a 10 were collected from Allergen Nomenclature and UniProt. B epitopes were predicted using AlgPred 2.0 and BepiPred 3.0. T epitopes were predicted with NetMHCIIpan 4.1 against 10 HLA-II alleles. Consensus epitopes were obtained through analysis and Epitope Cluster Analysis in the Immune Epitope Database. We found 7 B-cell epitopes and 28 linear T-cell epitopes binding to MHC II. A unique peptide (residues 160-174) exhibited overlap between linear B-cell and T-cell epitopes, highly conserved across tropomyosin sequences. These findings shed light on IgE cross-reactivity among the tested species. The described immuno-informatics pipeline and epitopes can inform in vitro research and guide synthetic multi-epitope proteins' design for potential allergology immunotherapies. Further in silico studies are warranted to confirm epitope accuracy and guide future experimental protocols.