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    Lupin allergy: Uncovering structural features and epitopes of ß-conglutin proteins in Lupinus Angustifolius L. with a focus on cross-allergenic reactivity to peanut and other legumes

    Access Status
    Fulltext not available
    Authors
    Jimenez-Lopez, J.
    Lima-Cabello, E.
    Melser, S.
    Foley, R.
    Singh, Karambir
    Alché Juan, D.
    Date
    2015
    Type
    Conference Paper
    
    Metadata
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    Citation
    Jimenez-Lopez, J. and Lima-Cabello, E. and Melser, S. and Foley, R. and Singh, K. and Alché Juan, D. 2015. Lupin allergy: Uncovering structural features and epitopes of ß-conglutin proteins in Lupinus Angustifolius L. with a focus on cross-allergenic reactivity to peanut and other legumes, in Proceedings of the Third International Conference IWBBIO 2015, Apr 15-17 2015, pp. 96-107. Granada, Spain: Springer.
    Source Title
    Lecture Notes in Computer Science (including subseries Lecture Notes in Artificial Intelligence and Lecture Notes in Bioinformatics)
    DOI
    10.1007/978-3-319-16483-0_10
    ISBN
    9783319164823
    School
    Centre for Crop Disease Management
    URI
    http://hdl.handle.net/20.500.11937/31368
    Collection
    • Curtin Research Publications
    Abstract

    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 ß-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 structural 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.

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