Lupin Allergy: Uncovering Structural Features and Epitopes of β-conglutin Proteins in Lupinus Angustifolius L. with a Focus on Cross-allergenic Reactivity to Peanut and Other Legumes [chapter]

José C. Jimenez-Lopez, Elena Lima-Cabello, Su Melser, Rhonda C. Foley, Karam B. Singh, Alché Juan D.
2015 Lecture Notes in Computer Science  
The use of sweet lupins as a new food is resulting in an increasing number of cases of allergy reactions, particularly in atopic patients with other pre-existing legume allergies. We performed an extensive in silico analysis of seed β-conglutins, a new family of major allergen proteins in lupin, and a comparison to other relevant food allergens such as Ara h 1. We analyzed surface residues involved in conformational epitopes, lineal B-and T-cell epitopes variability, and changes in 2-D
more » ... l elements and 3D motives, with the aim to investigate IgE-mediated cross-reactivity among lupin, peanut, and other different legumes. Our results revealed that considerable structural differences exist, particularly affecting 2-D elements (loops and coils), and numerous micro-heterogeneities are present in fundamental residues directly involved in epitopes variability. Variability of residues involved in IgE-binding epitopes might be a major contributor to the observed differences in cross-reactivity among legumes.
doi:10.1007/978-3-319-16483-0_10 fatcat:p2by4v26avbqhiu5fpzuibbkey