New findings by University of Virginia scientists, however, may allow for the development of more sensitive diagnostic tools and a better understanding of nut allergies.
The study, “Structural and Immunologic Characterization of Ara h 1, a Major Peanut Allergen,” appeared in the November 11 issue of the Journal of Biological Chemistry.Rethinking the Proteins
“In allergy diagnostics, using a recombinant protein is thought to reveal more consistent results, as they are more homogenous than natural proteins. Individual protein molecules purified from a natural source show much more variation at a molecular level from one another,” says Wladek Minor, PhD, professor of molecular physiology and biological physics in the UVA School of Medicine and study co-leader.
“However, people are exposed to allergens from natural sources, not recombinant protein,” he continues, “and people develop antibodies to different fragments of natural allergens. If there is a significant difference between a natural source and the recombinant allergen used for allergy diagnosis, the recombinant allergen is not a good replacement in the test, because different types of allergies can be overlooked.”
In their analysis, researchers also found strong similarities in the structure of the Ara h 1 protein and those of other plant-seed proteins, which could help explain why patients with peanut allergies frequently also have allergies to tree nuts such as walnuts, almonds, and cashews.
The team’s next steps in their research will be to determine exactly why peanut-allergic patients are often allergic to tree nuts as well, and to explain why peanut and tree-nut allergies are extremely difficult to outgrow, usually lasting a lifetime.
In addition to Minor, the international research team included Maksymilian Chruszcz, a member of Minor’s UVA research group; Soheila Maleki, from the U.S. Department of Agriculture; and Heimo Breiteneder, from the Medical University of Vienna. The multidisciplinary study included structural, bioinformatics, and immunological research on Ara h 1. Some methodology used in the project was developed as part of the NIH Protein Structure Initiative, and in particular the New York Structural Genomics Consortium.
Sally H. Jones | Newswise Science News
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