Literature DB >> 24253038

Structure and function of the peanut panallergen Ara h 8.

Barry K Hurlburt1, Lesa R Offermann, Jane K McBride, Karolina A Majorek, Soheila J Maleki, Maksymilian Chruszcz.   

Abstract

The incidence of peanut allergy continues to rise in the United States and Europe. Whereas exposure to the major allergens Ara h 1, 2, 3, and 6 can cause fatal anaphylaxis, exposure to the minor allergens usually does not. Ara h 8 is a minor allergen. Importantly, it is the minor food allergens that are thought to be responsible for oral allergy syndrome (OAS), in which sensitization to airborne allergens causes a Type 2 allergic reaction to ingested foods. Furthermore, it is believed that similar protein structure rather than a similar linear sequence is the cause of OAS. Bet v 1 from birch pollen is a common sensitizing agent, and OAS results when patients consume certain fruits, vegetables, tree nuts, and peanuts. Here, we report the three-dimensional structure of Ara h 8, a Bet v 1 homolog. The overall fold is very similar to that of Bet v 1, Api g 1 (celery), Gly m 4 (soy), and Pru av 1 (cherry). Ara h 8 binds the isoflavones quercetin and apigenin as well as resveratrol avidly.

Entities:  

Keywords:  Allergen; Antigen; Crystal Structure; Flavonoids; Fluorescence; Peanut

Mesh:

Substances:

Year:  2013        PMID: 24253038      PMCID: PMC3873548          DOI: 10.1074/jbc.M113.517797

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


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5.  CLANS: a Java application for visualizing protein families based on pairwise similarity.

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6.  Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier.

Authors:  Zora Marković-Housley; Massimo Degano; Doriano Lamba; Edda von Roepenack-Lahaye; Stephan Clemens; Markus Susani; Fátima Ferreira; Otto Scheiner; Heimo Breiteneder
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7.  Structure and lipid transport mechanism of a StAR-related domain.

Authors:  Y Tsujishita; J H Hurley
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8.  The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands.

Authors:  Jesper E Mogensen; Reinhard Wimmer; Jørgen N Larsen; Michael D Spangfort; Daniel E Otzen
Journal:  J Biol Chem       Date:  2002-04-12       Impact factor: 5.157

9.  Dominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by X-ray crystallography and site-directed mutagenesis.

Authors:  Michael D Spangfort; Osman Mirza; Henrik Ipsen; R J Joost Van Neerven; Michael Gajhede; Jørgen N Larsen
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6.  Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen.

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7.  A Quantitative Method for Detecting Ara h 2 by Generation and Utilization of Monoclonal Antibodies.

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Review 8.  Cross-reactivity of peanut allergens.

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9.  Impact of an N-terminal Polyhistidine Tag on Protein Thermal Stability.

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10.  Identification and in silico bioinformatics analysis of PR10 proteins in cashew nut.

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