Characterization of narrow-leaf lupin (Lupinus angustifolius L.) recombinant major allergen IgE-binding proteins and the natural ß-conglutin counterparts in sweet lupin seed species
© 2017 Elsevier Ltd ß-conglutin has been identified as a major allergen for Lupinus angustifolius seeds. The aim of this study was to evaluate the binding of IgE to five recombinant ß-conglutin isoforms (rß) that we overexpressed and purified and to their natural counterparts in different lupin spec...
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Journal Article |
| Published: |
Elsevier BV
2018
|
| Online Access: | http://hdl.handle.net/20.500.11937/61969 |
| _version_ | 1848760761055182848 |
|---|---|
| author | Jimenez-Lopez, J. Foley, R. Brear, E. Clarke, V. Lima-Cabello, E. Florido, J. Singh, Karam Alché, J. Smith, P. |
| author_facet | Jimenez-Lopez, J. Foley, R. Brear, E. Clarke, V. Lima-Cabello, E. Florido, J. Singh, Karam Alché, J. Smith, P. |
| author_sort | Jimenez-Lopez, J. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | © 2017 Elsevier Ltd ß-conglutin has been identified as a major allergen for Lupinus angustifolius seeds. The aim of this study was to evaluate the binding of IgE to five recombinant ß-conglutin isoforms (rß) that we overexpressed and purified and to their natural counterparts in different lupin species and cultivars. Western blotting suggested ß-conglutins were the main proteins responsible for the IgE reactivity of the lupin species and cultivars. Newly identified polypeptides from “sweet lupin” may constitute a potential new source of primary or cross-reactive sensitization to lupin, particularly to L. albus and L. angustifolius seed proteins. Several of them exhibited qualitative and quantitative differences in IgE-binding among these species and cultivars, mainly in sera from atopic patients that react to lupin rather than peanut. IgE-binding was more consistent to recombinant ß2 than to any of the other isoforms, making this protein a potential candidate for diagnosis and immunotherapy. |
| first_indexed | 2025-11-14T10:20:54Z |
| format | Journal Article |
| id | curtin-20.500.11937-61969 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T10:20:54Z |
| publishDate | 2018 |
| publisher | Elsevier BV |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-619692018-02-01T05:56:40Z Characterization of narrow-leaf lupin (Lupinus angustifolius L.) recombinant major allergen IgE-binding proteins and the natural ß-conglutin counterparts in sweet lupin seed species Jimenez-Lopez, J. Foley, R. Brear, E. Clarke, V. Lima-Cabello, E. Florido, J. Singh, Karam Alché, J. Smith, P. © 2017 Elsevier Ltd ß-conglutin has been identified as a major allergen for Lupinus angustifolius seeds. The aim of this study was to evaluate the binding of IgE to five recombinant ß-conglutin isoforms (rß) that we overexpressed and purified and to their natural counterparts in different lupin species and cultivars. Western blotting suggested ß-conglutins were the main proteins responsible for the IgE reactivity of the lupin species and cultivars. Newly identified polypeptides from “sweet lupin” may constitute a potential new source of primary or cross-reactive sensitization to lupin, particularly to L. albus and L. angustifolius seed proteins. Several of them exhibited qualitative and quantitative differences in IgE-binding among these species and cultivars, mainly in sera from atopic patients that react to lupin rather than peanut. IgE-binding was more consistent to recombinant ß2 than to any of the other isoforms, making this protein a potential candidate for diagnosis and immunotherapy. 2018 Journal Article http://hdl.handle.net/20.500.11937/61969 10.1016/j.foodchem.2017.10.015 Elsevier BV restricted |
| spellingShingle | Jimenez-Lopez, J. Foley, R. Brear, E. Clarke, V. Lima-Cabello, E. Florido, J. Singh, Karam Alché, J. Smith, P. Characterization of narrow-leaf lupin (Lupinus angustifolius L.) recombinant major allergen IgE-binding proteins and the natural ß-conglutin counterparts in sweet lupin seed species |
| title | Characterization of narrow-leaf lupin (Lupinus angustifolius L.) recombinant major allergen IgE-binding proteins and the natural ß-conglutin counterparts in sweet lupin seed species |
| title_full | Characterization of narrow-leaf lupin (Lupinus angustifolius L.) recombinant major allergen IgE-binding proteins and the natural ß-conglutin counterparts in sweet lupin seed species |
| title_fullStr | Characterization of narrow-leaf lupin (Lupinus angustifolius L.) recombinant major allergen IgE-binding proteins and the natural ß-conglutin counterparts in sweet lupin seed species |
| title_full_unstemmed | Characterization of narrow-leaf lupin (Lupinus angustifolius L.) recombinant major allergen IgE-binding proteins and the natural ß-conglutin counterparts in sweet lupin seed species |
| title_short | Characterization of narrow-leaf lupin (Lupinus angustifolius L.) recombinant major allergen IgE-binding proteins and the natural ß-conglutin counterparts in sweet lupin seed species |
| title_sort | characterization of narrow-leaf lupin (lupinus angustifolius l.) recombinant major allergen ige-binding proteins and the natural ß-conglutin counterparts in sweet lupin seed species |
| url | http://hdl.handle.net/20.500.11937/61969 |