The panel of egg allergens, Gal d 1-Gal d 5: Their improved purification and characterization

B. Jacobsen, K. Hoffmann-Sommergruber, T. T. Have, N. Foss, P. Briza, C. Oberhuber, C. Radauer, S. Alessandri, A.C. Knulst, M. Fernandez-Rivas, Vibeke Barkholt

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    Egg proteins represent one of the most important sources evoking food allergic reactions. In order to improve allergy diagnosis, purified and well-characterized proteins are needed. Although the egg white allergens Gal d 1, 2, 3 and 4 (ovomucoid, ovalbumin, ovotransferrin, and lysozyme) are commercially available, these preparations contain impurities, which affect exact in vitro diagnosis. The aim of the present study was to set up further purification protocols and to extend the characterization of the physicochemical and immunological properties of the final batches. The egg white allergens Gal d 1-4 were purified from commercial preparations, whereas Gal d 5 (a-livetin) was purified from egg yolk. The final batches of Gal d 1-5 consisted of a range of isoforms with defined tertiary structure. In addition, the IgE binding capacity of the purified egg allergens was tested using allergic patients' sera. The allergen batches will be further used to set up allergen specific diagnostic assays and to screen a larger collection of patients' sera.
    Original languageEnglish
    JournalMolecular Nutrition & Food Research
    Volume52
    Pages (from-to)S176-S185
    ISSN1613-4125
    DOIs
    Publication statusPublished - 2008

    Keywords

    • Egg
    • Allergens
    • Purification
    • NMR
    • pI

    Cite this

    Jacobsen, B. ; Hoffmann-Sommergruber, K. ; Have, T. T. ; Foss, N. ; Briza, P. ; Oberhuber, C. ; Radauer, C. ; Alessandri, S. ; Knulst, A.C. ; Fernandez-Rivas, M. ; Barkholt, Vibeke. / The panel of egg allergens, Gal d 1-Gal d 5: Their improved purification and characterization. In: Molecular Nutrition & Food Research. 2008 ; Vol. 52. pp. S176-S185.
    @article{fa03d3f0ad87466a95599938061570a3,
    title = "The panel of egg allergens, Gal d 1-Gal d 5: Their improved purification and characterization",
    abstract = "Egg proteins represent one of the most important sources evoking food allergic reactions. In order to improve allergy diagnosis, purified and well-characterized proteins are needed. Although the egg white allergens Gal d 1, 2, 3 and 4 (ovomucoid, ovalbumin, ovotransferrin, and lysozyme) are commercially available, these preparations contain impurities, which affect exact in vitro diagnosis. The aim of the present study was to set up further purification protocols and to extend the characterization of the physicochemical and immunological properties of the final batches. The egg white allergens Gal d 1-4 were purified from commercial preparations, whereas Gal d 5 (a-livetin) was purified from egg yolk. The final batches of Gal d 1-5 consisted of a range of isoforms with defined tertiary structure. In addition, the IgE binding capacity of the purified egg allergens was tested using allergic patients' sera. The allergen batches will be further used to set up allergen specific diagnostic assays and to screen a larger collection of patients' sera.",
    keywords = "Egg, Allergens, Purification, NMR, pI",
    author = "B. Jacobsen and K. Hoffmann-Sommergruber and Have, {T. T.} and N. Foss and P. Briza and C. Oberhuber and C. Radauer and S. Alessandri and A.C. Knulst and M. Fernandez-Rivas and Vibeke Barkholt",
    year = "2008",
    doi = "10.1002/mnfr.200700414",
    language = "English",
    volume = "52",
    pages = "S176--S185",
    journal = "Molecular Nutrition & Food Research",
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    Jacobsen, B, Hoffmann-Sommergruber, K, Have, TT, Foss, N, Briza, P, Oberhuber, C, Radauer, C, Alessandri, S, Knulst, AC, Fernandez-Rivas, M & Barkholt, V 2008, 'The panel of egg allergens, Gal d 1-Gal d 5: Their improved purification and characterization', Molecular Nutrition & Food Research, vol. 52, pp. S176-S185. https://doi.org/10.1002/mnfr.200700414

    The panel of egg allergens, Gal d 1-Gal d 5: Their improved purification and characterization. / Jacobsen, B.; Hoffmann-Sommergruber, K.; Have, T. T.; Foss, N.; Briza, P.; Oberhuber, C.; Radauer, C.; Alessandri, S.; Knulst, A.C.; Fernandez-Rivas, M.; Barkholt, Vibeke.

    In: Molecular Nutrition & Food Research, Vol. 52, 2008, p. S176-S185.

    Research output: Contribution to journalJournal articleResearchpeer-review

    TY - JOUR

    T1 - The panel of egg allergens, Gal d 1-Gal d 5: Their improved purification and characterization

    AU - Jacobsen, B.

    AU - Hoffmann-Sommergruber, K.

    AU - Have, T. T.

    AU - Foss, N.

    AU - Briza, P.

    AU - Oberhuber, C.

    AU - Radauer, C.

    AU - Alessandri, S.

    AU - Knulst, A.C.

    AU - Fernandez-Rivas, M.

    AU - Barkholt, Vibeke

    PY - 2008

    Y1 - 2008

    N2 - Egg proteins represent one of the most important sources evoking food allergic reactions. In order to improve allergy diagnosis, purified and well-characterized proteins are needed. Although the egg white allergens Gal d 1, 2, 3 and 4 (ovomucoid, ovalbumin, ovotransferrin, and lysozyme) are commercially available, these preparations contain impurities, which affect exact in vitro diagnosis. The aim of the present study was to set up further purification protocols and to extend the characterization of the physicochemical and immunological properties of the final batches. The egg white allergens Gal d 1-4 were purified from commercial preparations, whereas Gal d 5 (a-livetin) was purified from egg yolk. The final batches of Gal d 1-5 consisted of a range of isoforms with defined tertiary structure. In addition, the IgE binding capacity of the purified egg allergens was tested using allergic patients' sera. The allergen batches will be further used to set up allergen specific diagnostic assays and to screen a larger collection of patients' sera.

    AB - Egg proteins represent one of the most important sources evoking food allergic reactions. In order to improve allergy diagnosis, purified and well-characterized proteins are needed. Although the egg white allergens Gal d 1, 2, 3 and 4 (ovomucoid, ovalbumin, ovotransferrin, and lysozyme) are commercially available, these preparations contain impurities, which affect exact in vitro diagnosis. The aim of the present study was to set up further purification protocols and to extend the characterization of the physicochemical and immunological properties of the final batches. The egg white allergens Gal d 1-4 were purified from commercial preparations, whereas Gal d 5 (a-livetin) was purified from egg yolk. The final batches of Gal d 1-5 consisted of a range of isoforms with defined tertiary structure. In addition, the IgE binding capacity of the purified egg allergens was tested using allergic patients' sera. The allergen batches will be further used to set up allergen specific diagnostic assays and to screen a larger collection of patients' sera.

    KW - Egg

    KW - Allergens

    KW - Purification

    KW - NMR

    KW - pI

    U2 - 10.1002/mnfr.200700414

    DO - 10.1002/mnfr.200700414

    M3 - Journal article

    VL - 52

    SP - S176-S185

    JO - Molecular Nutrition & Food Research

    JF - Molecular Nutrition & Food Research

    SN - 1613-4125

    ER -