Submitted to: Foods
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 11/19/2019
Publication Date: 11/22/2019
Citation: Mcbride, J.K., Cheng, H., Maleki, S.J., Hurlburt, B.K. 2019. Purification and characterization of pathogenesis related class 10 panallergens. Foods. 8:609-623. https://doi.org/10.3390/foods8120609.
Interpretive Summary: Oral allergy syndrome (OAS) describes an allergic reaction where an individual sensitized by pollen allergens develops symptoms after eating certain foods. These reactions are usually mild and involve the oral cavity. Certain proteins in pollen and fruits, vegetables and nuts are responsible for this reaction. In this work we characterize a subset of these proteins for function and structure. Small hydrophobic chemicals that are found in all plants were found to bind to these proteins. The structures of these proteins were all found to be nearly identical.
Technical Abstract: Oral allergy syndrome (OAS) describes an allergic reaction where an individual sensitized by pollen allergens develops symptoms after eating certain foods. In northern Europe and the US, OAS is caused by cross-reactivity among a class of proteins ubiquitous in plants called pathogenesis related class 10 proteins (PR-10 proteins). The best characterized of these proteins is Bet v 1 from birch pollen and its primary function in plants is thought to be the binding of hydrophobic ligands. To further our understanding of the structure, function and immunological reactivity of these proteins, we cloned a subset of seven recombinant PR-10 proteins from pollens, peanuts and hazelnuts and developed a standard purification method for them. IgE binding of purified PR-10 proteins was analyzed by ImmunoCAP ISAC microarray and enzyme-linked immunosorbent assays (ELISAs) with sera from allergic patients. We investigated the binding activities of PR10s by testing 16 different ligands with each recombinant protein. We compared the secondary structures of all proteins using circular dichroism (CD). Overall, the PR-10s in this study had very similar structures and ligand binding preferences, but bound IgE with very different affinities. We suggest our protocol has the potential to be a near-universal method for PR-10 purification that will facilitate further research into this important class of panallergens.