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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Food Processing and Sensory Quality Research » Research » Publications at this Location » Publication #303339
Title: The molecular basis of peanut allergy

Author
item MUELLER, GEOFFREY - National Institute Of Environmental Health Sciences (NIEHS, NIH)
item Maleki, Soheila
item PEDERSEN, LARS - National Institute Of Environmental Health Sciences (NIEHS, NIH)

Submitted to: Current Allergy and Asthma Reports
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/28/2014
Publication Date: 9/13/2013
Citation: Mueller, G.A., Maleki, S.J., Pedersen, L.C. 2013. The molecular basis of peanut allergy. Current Allergy and Asthma Reports. 14:429.

Interpretive Summary: Peanut allergens can trigger a potent and sometimes dangerous immune response in an increasing number of people. The molecular structures of these allergens form the basis for understanding this response. This review describes the currently known peanut allergen structures, and discusses how modifications both by the plant and via processing can affect digestion, immune system recognition, and the interaction of immunoglobulin E (IgE) antibody from the blood of peanut allergic individuals with the allergen molecules. The allergen structures help explain cross-reactivity (allergic reaction of an individual to multiple nut allergens) among allergens from different sources, which is useful in improving patient diagnostics. Surprisingly, it was recently noted that related short peptide sequences among peanut allergens could also be a source of cross-reactivity. The molecular features of peanut allergens continue to inform predictions and provide new research directions in the study of allergic disease.

Technical Abstract: Peanut allergens can trigger a potent and sometimes dangerous immune response in an increasing number of people. The molecular structures of these allergens form the basis for understanding this response. This review describes the currently known peanut allergen structures, and discusses how modifications both enzymatic and non-enzymatic affect digestion, innate immune recognition, and IgE interactions. The allergen structures help explain cross-reactivity among allergens from different sources, which is useful in improving patient diagnostics. Surprisingly, it was recently noted that related short peptide sequences among peanut allergens could also be a source of cross-reactivity. The molecular features of peanut allergens continue to inform predictions, and provide new research directions in the study of allergic disease.