Journal of Agricultural and Food Chemistry · 2006 · 75 citations · 20 references
Life SciencesImmunologyMolecular BiologyAllergyHypersensitivityImmunogeneticsAllergen RecognitionAllergic DiseaseFood AllergensFood AllergyIge-mediated AllergyTree Nut AllergyAntibody Cross-reactivityImmune Cross-reactivityMolecular Basis Of AllergenicityRecombinant Fusion ProteinsSequence HomologyTree Nut Allergen IdentificationTree Nut Cross-reactivityWalnut Allergy
Allergy to walnut is the most frequently reported tree nut allergy in the United States. Walnut 2S albumin, a vicilin-like protein, and a lipid transfer protein allergen have previously been described. Our objective was to clone and express a cDNA encoding a legumin group protein, assess IgE-binding with sera from walnut allergic patients, and investigate cross-reactivity with selected nuts. Primers were used to obtain the cDNA by 5' and 3' rapid amplification of cDNA ends from walnut mRNA. The cDNA was subcloned into the pMAL-c2X vector and the recombinant fusion protein, named rJug r 4, was expressed in Escherichia coli. The obtained cDNA encoded a precursor protein with a predicted molecular weight of 58.1 kD, which showed significant sequence homology to hazelnut and cashew legumin allergens. Serum IgE from 21 of 37 (57%) patients bound the rJug r 4 fusion protein. In vitro cross-reactivity was demonstrated with hazelnut, cashew, and peanut protein extracts.
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Molecular cloning and epitope analysis of the peanut allergen Ara h 3
Pat Rabjohn, Erica M. Helm, J. Steven Stanley et al. · Journal of Clinical Investigation · 1999 · 413 citations · Full text