Abstract

Results We have demonstrated that boiling decrease solubility and IgE reactivity of PBS-extracted rice and wheat proteins, but in SDS-extracts this reactivity was only slightly affected. The sera of patients highly positive on the IgE immunoblot, positive in basophil activation and skin prick test with boiled rice components were used for characterizing the IgE-binding proteins separated by 1-D or 2-D electrophoresis. Employing mass spectrometry, we identified 22 rice SDS soluble proteins. Six of them were new potential rice allergens: glutelin C precursor, granulebound starch synthase 1 protein, disulfide isomerase-like 1-1 protein, hypothetical protein OsI_13867, putative acid phosphatase precursor 1, and a protein encoded by locus Os02g0453600. These proteins retaining IgE-binding capacity also after thermal processing potentially represent important allergens in rice-containing foodstuffs. All of the identified rice proteins differed from known wheat allergens, except proteins belonging to the a amylase/trypsin-inhibitor family.

Highlights

  • Similarity among food allergens is a great problem affecting the specificity of diagnosis and treatment of allergic patients

  • Rice proteins recognized by immunoglobulin E antibodies of patients with food allergies Ludmila Tuckova1*, Jaroslav Goliáš1, Zuzana Humlová2, Petr Halada3, Vìra Hábová1, Ivana Janatková4

  • The PBS-soluble and SDS-soluble proteins were analyzed by 1- or 2-DE and IgE binding components were characterized by immunoblot, basophil activation test, skin prick test and identified by MALDI-TOF mass spectrometry techniques

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Summary

Open Access

Rice proteins recognized by immunoglobulin E antibodies of patients with food allergies Ludmila Tuckova1*, Jaroslav Goliáš, Zuzana Humlová, Petr Halada, Vìra Hábová, Ivana Janatková. From 5th International Symposium on Molecular Allergology (ISMA 2013) Vienna, Austria. From 5th International Symposium on Molecular Allergology (ISMA 2013) Vienna, Austria. 6-7 December 2013

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