Physical interaction between the strawberry allergen Fra a 1 and an associated partner FaAP: Interaction of Fra a 1 proteins and FaAP. Issue 10 (14th July 2017)

• Record Type: Journal Article
• Authors: Franz‐Oberdorf, Katrin; Langer, Andreas; Strasser, Ralf; Isono, Erika; Ranftl, Quirin L.; Wunschel, Christian; Schwab, Wilfried
• Is Part Of: Proteins. Volume 85:Issue 10(2017)
• Page Start: 1891
• Page End: 1901
• Publication Date: 2017-07-14
• Subjects: abscisic acid (ABA) -- allergen -- dimerization -- Fra a 1‐Associated Protein (FaAP) -- plant defense -- protein–protein interaction -- PR‐10 protein family -- strawberry allergen Fra a 1.01E/1.02/1.03 -- time resolved DNA‐switching measurements -- yeast two‐hybrid; Proteins -- Periodicals; Proteins -- Periodicals; 572.6
• DOI: 10.1002/prot.25343
• Languages: English
• ISSNs: 0887-3585

Abstract

Abstract: 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 M al d 1‐ A ssociated P rotein has been previously identified as interaction partner of Mal d 1 we studied the binding of the orthologous F ra a 1‐ A ssociated P rotein (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.