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
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...
| Main Authors: | , , , , , |
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| Format: | Conference Paper |
| Published: |
2015
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| Online Access: | http://hdl.handle.net/20.500.11937/31368 |
| _version_ | 1848753360357818368 |
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| author | Jimenez-Lopez, J. Lima-Cabello, E. Melser, S. Foley, R. Singh, Karambir Alché Juan, D. |
| author_facet | Jimenez-Lopez, J. Lima-Cabello, E. Melser, S. Foley, R. Singh, Karambir Alché Juan, D. |
| author_sort | Jimenez-Lopez, J. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-14T08:23:17Z |
| format | Conference Paper |
| id | curtin-20.500.11937-31368 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T08:23:17Z |
| publishDate | 2015 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-313682017-09-19T07:42:10Z 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 Jimenez-Lopez, J. Lima-Cabello, E. Melser, S. Foley, R. Singh, Karambir Alché Juan, D. 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. 2015 Conference Paper http://hdl.handle.net/20.500.11937/31368 10.1007/978-3-319-16483-0_10 restricted |
| spellingShingle | Jimenez-Lopez, J. Lima-Cabello, E. Melser, S. Foley, R. Singh, Karambir Alché Juan, D. 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 |
| title | 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 |
| title_full | 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 |
| title_fullStr | 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 |
| title_full_unstemmed | 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 |
| title_short | 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 |
| title_sort | 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 |
| url | http://hdl.handle.net/20.500.11937/31368 |