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The identification of allergen proteins in sugar beet (Beta vulgaris) pollen causing occupational allergy in greenhouses.

Luoto, Susanne; Lambert, Wietske LU ; Blomqvist, Anna and Emanuelsson, Cecilia LU (2008) In Clinical and Molecular Allergy 6(1).
Abstract
ABSTRACT: BACKGROUND: During production of sugar beet (Beta vulgaris) seeds in greenhouses, workers frequently develop allergic symptoms. The aim of this study was to identify and characterize possible allergens in sugar beet pollen. METHODS: 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. RESULTS: 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... (More)
ABSTRACT: BACKGROUND: During production of sugar beet (Beta vulgaris) seeds in greenhouses, workers frequently develop allergic symptoms. The aim of this study was to identify and characterize possible allergens in sugar beet pollen. METHODS: 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. RESULTS: 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 Chenopodium album. 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. CONCLUSION: Two occupational allergens were identified in sugar beet pollen showing sequence similarity with Chenopodium 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 Chenopodium pollinosis, immunotherapy with sugar beet pollen extracts may be feasible. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Clinical and Molecular Allergy
volume
6
issue
1
publisher
BioMed Central
external identifiers
  • pmid:18694503
  • scopus:50649100504
ISSN
1476-7961
DOI
10.1186/1476-7961-6-7
language
English
LU publication?
yes
id
acf34032-4f47-4104-bad0-e232bfe3cb6b (old id 1223300)
date added to LUP
2008-10-20 10:26:50
date last changed
2017-09-17 06:13:55
@article{acf34032-4f47-4104-bad0-e232bfe3cb6b,
  abstract     = {ABSTRACT: BACKGROUND: During production of sugar beet (Beta vulgaris) seeds in greenhouses, workers frequently develop allergic symptoms. The aim of this study was to identify and characterize possible allergens in sugar beet pollen. METHODS: 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. RESULTS: 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 Chenopodium album. 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. CONCLUSION: Two occupational allergens were identified in sugar beet pollen showing sequence similarity with Chenopodium 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 Chenopodium pollinosis, immunotherapy with sugar beet pollen extracts may be feasible.},
  articleno    = {7},
  author       = {Luoto, Susanne and Lambert, Wietske and Blomqvist, Anna and Emanuelsson, Cecilia},
  issn         = {1476-7961},
  language     = {eng},
  number       = {1},
  publisher    = {BioMed Central},
  series       = {Clinical and Molecular Allergy},
  title        = {The identification of allergen proteins in sugar beet (Beta vulgaris) pollen causing occupational allergy in greenhouses.},
  url          = {http://dx.doi.org/10.1186/1476-7961-6-7},
  volume       = {6},
  year         = {2008},
}