6STB
Crystal structure of the strawberry pathogenesis-related 10 (PR-10) Fra a 1.02 protein, Q64W mutant
Summary for 6STB
Entry DOI | 10.2210/pdb6stb/pdb |
Related | 5AMW |
Descriptor | Major strawberry allergen Fra a 1-2 (2 entities in total) |
Functional Keywords | fragaria x ananassa, fra a 1, allergen, fruit, ripening, pr-10 |
Biological source | Fragaria ananassa (Strawberry) |
Total number of polymer chains | 2 |
Total formula weight | 35556.21 |
Authors | Orozco-Navarrete, B.,Kaczmarska, Z.,Dupeux, F.,Pott, D.,Diaz Perales, A.,Casanal, A.,Marquez, J.A.,Valpuesta, V.,Merchante, C. (deposition date: 2019-09-10, release date: 2019-12-18, Last modification date: 2024-01-24) |
Primary citation | Orozco-Navarrete, B.,Kaczmarska, Z.,Dupeux, F.,Garrido-Arandia, M.,Pott, D.,Perales, A.D.,Casanal, A.,Marquez, J.A.,Valpuesta, V.,Merchante, C. Structural Bases for the Allergenicity of Fra a 1.02 in Strawberry Fruits. J.Agric.Food Chem., 68:10951-10961, 2020 Cited by PubMed Abstract: Although 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 cross-reacts 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. PubMed: 31774998DOI: 10.1021/acs.jafc.9b05714 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.27 Å) |
Structure validation
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