Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 401450
Title Cross-reactivity between peanut and lupin proteins
Author(s) Sirtori, E.; Resta, D.; Arnoldi, A.; Savelkoul, H.F.J.; Wichers, H.J.
Source Food Chemistry 126 (2011)3. - ISSN 0308-8146 - p. 902 - 910.
DOI http://dx.doi.org/10.1016/j.foodchem.2010.11.073
Department(s) Cell Biology and Immunology
FBR Fresh Supply Chains
Food Chemistry Group
VLAG
WIAS
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) ige-binding - primary sensitization - food allergens - flour - anaphylaxis - asthma - child - risk - seed - inhalation
Abstract Peanut-allergic individuals may also react to lupin, which, for this reason, has been included in the EU list of food allergens. Since there is not yet any general consensus on the major allergen/s in lupin, the objective of this investigation was to compare the reactivity of the main lupin proteins towards the IgE of the sera of allergic patients. Both Lupinus albus and Lupinus angustifolius were investigated. ELISA’s, Western blotting and mass spectrometry, including also de novo sequencing of the unknown lupin proteins, were used for identifying the IgE-binding proteins. Significant differences in the protein reactivities were observed. In particular, there was a direct relationship between the level of peanut-specific IgE’s and the cross-reactivity to lupin proteins; also the reactivity of each serum appeared to be unique. Although numerous lupin proteins bind IgE’s, our data suggest a predominant contribution of a-conglutin in the reactivity of both L. albus and L. angustifolius.
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