The identification of allergen proteins in sugar beet (<it>Beta vulgaris</it>) pollen causing occupational allergy in greenhouses
<p>Abstract</p> <p>Background</p> <p>During production of sugar beet (<it>Beta vulgaris</it>) seeds in greenhouses, workers frequently develop allergic symptoms. The aim of this study was to identify and characterize possible allergens in sugar beet pollen.&...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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BMC
2008-08-01
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| Series: | Clinical and Molecular Allergy |
| Online Access: | http://www.clinicalmolecularallergy.com/content/6/1/7 |
| _version_ | 1818790152315600896 |
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| author | Blomqvist Anna Lambert Wietske Luoto Susanne Emanuelsson Cecilia |
| author_facet | Blomqvist Anna Lambert Wietske Luoto Susanne Emanuelsson Cecilia |
| author_sort | Blomqvist Anna |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>During production of sugar beet (<it>Beta vulgaris</it>) seeds in greenhouses, workers frequently develop allergic symptoms. The aim of this study was to identify and characterize possible allergens in sugar beet pollen.</p> <p>Methods</p> <p>Sera from individuals at a local sugar beet seed producing company, having positive SPT and specific IgE to sugar beet pollen extract, were used for immunoblotting. Proteins in sugar beet pollen extracts were separated by 1- and 2-dimensional electrophoresis, and IgE-reactive proteins analyzed by liquid chromatography tandem mass spectrometry.</p> <p>Results</p> <p>A 14 kDa protein was identified as an allergen, since IgE-binding was inhibited by the well-characterized allergen Che a 2, profilin, from the related species <it>Chenopodium album</it>. The presence of 17 kDa and 14 kDa protein homologues to both the allergens Che a 1 and Che a 2 were detected in an extract from sugar beet pollen, and partial amino acid sequences were determined, using inclusion lists for tandem mass spectrometry based on homologous sequences.</p> <p>Conclusion</p> <p>Two occupational allergens were identified in sugar beet pollen showing sequence similarity with <it>Chenopodium </it>allergens. Sequence data were obtained by mass spectrometry (70 and 25%, respectively for Beta v 1 and Beta v 2), and can be used for cloning and recombinant expression of the allergens. As for treatment of <it>Chenopodium </it>pollinosis, immunotherapy with sugar beet pollen extracts may be feasible.</p> |
| first_indexed | 2024-12-18T14:50:55Z |
| format | Article |
| id | doaj.art-5a2c877036794e61a91823326a429ac0 |
| institution | Directory Open Access Journal |
| issn | 1476-7961 |
| language | English |
| last_indexed | 2024-12-18T14:50:55Z |
| publishDate | 2008-08-01 |
| publisher | BMC |
| record_format | Article |
| series | Clinical and Molecular Allergy |
| spelling | doaj.art-5a2c877036794e61a91823326a429ac02022-12-21T21:04:11ZengBMCClinical and Molecular Allergy1476-79612008-08-0161710.1186/1476-7961-6-7The identification of allergen proteins in sugar beet (<it>Beta vulgaris</it>) pollen causing occupational allergy in greenhousesBlomqvist AnnaLambert WietskeLuoto SusanneEmanuelsson Cecilia<p>Abstract</p> <p>Background</p> <p>During production of sugar beet (<it>Beta vulgaris</it>) seeds in greenhouses, workers frequently develop allergic symptoms. The aim of this study was to identify and characterize possible allergens in sugar beet pollen.</p> <p>Methods</p> <p>Sera from individuals at a local sugar beet seed producing company, having positive SPT and specific IgE to sugar beet pollen extract, were used for immunoblotting. Proteins in sugar beet pollen extracts were separated by 1- and 2-dimensional electrophoresis, and IgE-reactive proteins analyzed by liquid chromatography tandem mass spectrometry.</p> <p>Results</p> <p>A 14 kDa protein was identified as an allergen, since IgE-binding was inhibited by the well-characterized allergen Che a 2, profilin, from the related species <it>Chenopodium album</it>. The presence of 17 kDa and 14 kDa protein homologues to both the allergens Che a 1 and Che a 2 were detected in an extract from sugar beet pollen, and partial amino acid sequences were determined, using inclusion lists for tandem mass spectrometry based on homologous sequences.</p> <p>Conclusion</p> <p>Two occupational allergens were identified in sugar beet pollen showing sequence similarity with <it>Chenopodium </it>allergens. Sequence data were obtained by mass spectrometry (70 and 25%, respectively for Beta v 1 and Beta v 2), and can be used for cloning and recombinant expression of the allergens. As for treatment of <it>Chenopodium </it>pollinosis, immunotherapy with sugar beet pollen extracts may be feasible.</p>http://www.clinicalmolecularallergy.com/content/6/1/7 |
| spellingShingle | Blomqvist Anna Lambert Wietske Luoto Susanne Emanuelsson Cecilia The identification of allergen proteins in sugar beet (<it>Beta vulgaris</it>) pollen causing occupational allergy in greenhouses Clinical and Molecular Allergy |
| title | The identification of allergen proteins in sugar beet (<it>Beta vulgaris</it>) pollen causing occupational allergy in greenhouses |
| title_full | The identification of allergen proteins in sugar beet (<it>Beta vulgaris</it>) pollen causing occupational allergy in greenhouses |
| title_fullStr | The identification of allergen proteins in sugar beet (<it>Beta vulgaris</it>) pollen causing occupational allergy in greenhouses |
| title_full_unstemmed | The identification of allergen proteins in sugar beet (<it>Beta vulgaris</it>) pollen causing occupational allergy in greenhouses |
| title_short | The identification of allergen proteins in sugar beet (<it>Beta vulgaris</it>) pollen causing occupational allergy in greenhouses |
| title_sort | identification of allergen proteins in sugar beet it beta vulgaris it pollen causing occupational allergy in greenhouses |
| url | http://www.clinicalmolecularallergy.com/content/6/1/7 |
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