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Research Article Free access | 10.1172/JCI118216

Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity.

A W Burks, G Cockrell, J S Stanley, R M Helm, and G A Bannon

Department of Pediatrics, University of Arkansas for Medical Sciences, Little Rock 72205, USA.

Find articles by Burks, A. in: JCI | PubMed | Google Scholar

Department of Pediatrics, University of Arkansas for Medical Sciences, Little Rock 72205, USA.

Find articles by Cockrell, G. in: JCI | PubMed | Google Scholar

Department of Pediatrics, University of Arkansas for Medical Sciences, Little Rock 72205, USA.

Find articles by Stanley, J. in: JCI | PubMed | Google Scholar

Department of Pediatrics, University of Arkansas for Medical Sciences, Little Rock 72205, USA.

Find articles by Helm, R. in: JCI | PubMed | Google Scholar

Department of Pediatrics, University of Arkansas for Medical Sciences, Little Rock 72205, USA.

Find articles by Bannon, G. in: JCI | PubMed | Google Scholar

Published October 1, 1995 - More info

Published in Volume 96, Issue 4 on October 1, 1995
J Clin Invest. 1995;96(4):1715–1721. https://doi.org/10.1172/JCI118216.
© 1995 The American Society for Clinical Investigation
Published October 1, 1995 - Version history
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Abstract

Peanut allergy is a significant health problem because of the frequency, the potential severity, and the chronicity of the allergic sensitivity. Serum IgE from patients with documented peanut hypersensitivity reactions and a peanut cDNA expression library were used to identify clones that encode peanut allergens. One of the major peanut allergens, Ara h I, was selected from these clones using Ara h I specific oligonucleotides and polymerase chain reaction technology. The Ara h I clone identified a 2.3-kb mRNA species on a Northern blot containing peanut poly (A)+ RNA. DNA sequence analysis of the cloned inserts revealed that the Ara h I allergen has significant homology with the vicilin seed storage protein family found in most higher plants. The isolation of the Ara h I clones allowed the synthesis of this protein in E. coli cells and subsequent recognition of this recombinant protein in immunoblot analysis using serum IgE from patients with peanut hypersensitivity. With the production of the recombinant peanut protein it will now be possible to address the pathophysiologic and immunologic mechanisms regarding peanut hypersensitivity reactions specifically and food hypersensitivity in general

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