Publikation: Physical interaction between the strawberry allergen Fra a 1 and an associated partner FaAP : Interaction of Fra a 1 proteins and FaAP
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The strawberry fruit allergens Fra a 1.01E, Fra a 1.02 and Fra a 1.03 belong to the group of pathogenesis-related 10 (PR-10) proteins and are homologs of the major birch pollen Bet v 1 and apple allergen Mal d 1. Bet v 1 related proteins are the most extensively studied allergens but their physiological function in planta remains elusive. Since Mal d 1-Associated Protein has been previously identified as interaction partner of Mal d 1 we studied the binding of the orthologous Fra a 1-Associated Protein (FaAP) to Fra a 1.01E/1.02/1.03. As the C-terminal sequence of FaAP showed strong auto-activation activity in yeast 2-hybrid analysis a novel time resolved DNA-switching system was successfully applied. Fra a 1.01E, Fra a 1.02, and Fra a 1.03 bind to FaAP with KD of 4.5 ± 1.1, 15 ± 3, and 11 ± 2 nM, respectively. Fra a 1.01E forms a dimer, whereas Fra a 1.02 and Fra a 1.03 bind as monomer. The results imply that PR-10 proteins might be integrated into a protein-interaction network and FaAP binding appears to be essential for the physiological function of the Fra a 1 proteins.
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FRANZ-OBERDORF, Katrin, Andreas LANGER, Ralf STRASSER, Erika ISONO, Quirin L. RANFTL, Christian WUNSCHEL, Wilfried SCHWAB, 2017. Physical interaction between the strawberry allergen Fra a 1 and an associated partner FaAP : Interaction of Fra a 1 proteins and FaAP. In: Proteins : Structure, Function, and Bioinformatics. 2017, 85(10), pp. 1891-1901. ISSN 0887-3585. eISSN 1097-0134. Available under: doi: 10.1002/prot.25343BibTex
@article{FranzOberdorf2017-10Physi-39858,
year={2017},
doi={10.1002/prot.25343},
title={Physical interaction between the strawberry allergen Fra a 1 and an associated partner FaAP : Interaction of Fra a 1 proteins and FaAP},
number={10},
volume={85},
issn={0887-3585},
journal={Proteins : Structure, Function, and Bioinformatics},
pages={1891--1901},
author={Franz-Oberdorf, Katrin and Langer, Andreas and Strasser, Ralf and Isono, Erika and Ranftl, Quirin L. and Wunschel, Christian and Schwab, Wilfried}
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<dcterms:abstract xml:lang="eng">The strawberry fruit allergens Fra a 1.01E, Fra a 1.02 and Fra a 1.03 belong to the group of pathogenesis-related 10 (PR-10) proteins and are homologs of the major birch pollen Bet v 1 and apple allergen Mal d 1. Bet v 1 related proteins are the most extensively studied allergens but their physiological function in planta remains elusive. Since Mal d 1-Associated Protein has been previously identified as interaction partner of Mal d 1 we studied the binding of the orthologous Fra a 1-Associated Protein (FaAP) to Fra a 1.01E/1.02/1.03. As the C-terminal sequence of FaAP showed strong auto-activation activity in yeast 2-hybrid analysis a novel time resolved DNA-switching system was successfully applied. Fra a 1.01E, Fra a 1.02, and Fra a 1.03 bind to FaAP with KD of 4.5 ± 1.1, 15 ± 3, and 11 ± 2 nM, respectively. Fra a 1.01E forms a dimer, whereas Fra a 1.02 and Fra a 1.03 bind as monomer. The results imply that PR-10 proteins might be integrated into a protein-interaction network and FaAP binding appears to be essential for the physiological function of the Fra a 1 proteins.</dcterms:abstract>
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