Using the A-RISC index to predict IgE cross-reactivity in legume allergens An in silico approach
Main Article Content
Keywords
Cross-reactivity, food allergy, IN SILICO, Allergy to Legumes, Component resolved diagnosis
Abstract
Introduction: Legumes are a common source of allergic sensitization in many regions worldwide. Structural similarity among homologous proteins can lead to IgE-mediated cross-reactivity. In this context, in silico analysis offers a valuable approach to predict potential molecular interactions among related allergens and to support the interpretation of risk in patients with multiple sensitizations.
Methods: An in silico analysis was conducted to evaluate sequence homology, structural conservation, and surface exposure of IgE epitopes across five major protein families: 11S globulins, 7S globulins, 2S albumins, nsLTPs, and PR-10. Tools included multiple sequence alignment, A-RISC index calculation, and 3D visualization with ChimeraX.
Results: PR-10 proteins exhibited high homology (A-RISC >0.75), suggesting a high risk of cross-reactivity. Vicilins and glycinins showed intermediate similarity (A-RISC 0.45–0.57), while nsLTPs and 2S albumins displayed low A-RISC values (<0.50), although conserved structural motifs were identified in immunologically relevant regions.
Conclusion: This in silico approach enables early identification of cross-reactivity potential, reinforces the value of component-resolved molecular diagnostics, and contributes to improved food labeling, clinical decision-making, and nutritional safety in patients with multiple sensitizations.
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