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Physical interaction between the strawberry allergen Fra a 1 and an associated partner FaAP: Interaction of Fra a 1 proteins and FaAP
Author(s) -
FranzOberdorf Katrin,
Langer Andreas,
Strasser Ralf,
Isono Erika,
Ranftl Quirin L.,
Wunschel Christian,
Schwab Wilfried
Publication year - 2017
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25343
Subject(s) - chemistry , yeast , function (biology) , dimer , plasma protein binding , computational biology , protein–protein interaction , genetics , biochemistry , biology , organic chemistry
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 K D 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.