6st8
From Proteopedia
Crystal structure of the strawberry pathogenesis-related 10 (PR-10) Fra a 1.02 protein
Structural highlights
FunctionFRA12_FRAAN Involved in the control of flavonoid biosynthesis in fruits, probably by binding directly to natural flavonoids (By similarity). Binds the natural flavonoid myricetin with affinities in the low micromolar range (PubMed:24133217).[UniProtKB:D0E0C7][1] Publication Abstract from PubMedAlthough strawberries are highly appreciated fruits, their intake can induce allergic reactions in atopic patients. These reactions can be due to the patient s previous sensitization to the major birch-pollen allergen Bet v 1, by which, IgE generated in response to Bet v 1 crossreacts with the structurally-related strawberry Fra a 1 protein family. Fra a 1.02 is the most expressed paralog in ripe strawberries and is highly allergenic. To better understand the molecular mechanisms regulating this allergic response, we have determined the three-dimensional structure of Fra a 1.02 and four site-directed mutants that were designed based on their positions in potential epitopes. Fra a 1.02 and mutants conform to the START fold. We show that the cross-reactivity of all the mutant variants to IgE from patients allergic to Bet v 1 was significantly reduced without altering the conserved structural fold, so that they could potentially be used as hypoallergenic Fra a 1 variants for the generation of vaccines against strawberry allergy in atopic patients. STRUCTURAL BASIS FOR THE ALLERGENICITY OF Fra a 1.02 IN STRAWBERRY FRUITS.,Orozco-Navarrete B, Kaczmarska Z, Dupeux F, Garrido-Aranda M, Pott D, Diaz-Perales A, Casanal A, Marquez JA, Valpuesta V, Merchante C J Agric Food Chem. 2019 Nov 27. doi: 10.1021/acs.jafc.9b05714. PMID:31774998[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
