Structural highlights
FunctionPublication Abstract from PubMedKiwifruits have become one of the most common food sources triggering allergic reactions. In patients suffering from birch pollen related food allergy, reactions result from initial sensitization to the birch (Betula verrucosa) pollen allergen Bet v 1, followed by immunological cross-reactivity to structurally homologous proteins in kiwifruit. Clinical symptoms range from scratching and itching of the oral cavity to more severe immunological reactions such as rhino conjunctivitis. In this work we assigned backbone and side chain (1)H, (13)C and (15)N chemical shifts of the 17 kDa PR-10 allergens Act c 8.0101 and Act d 8.0101 from golden (Actinidia chinesis) and green (Actinidia deliciosa) kiwifruit by solution NMR spectroscopy. The chemical shift data confirm the characteristic Bet v 1 fold for both proteins, consisting of a seven-stranded antiparallel beta-sheet interrupted by two short alpha-helices, along with a long C-terminal alpha-helix. Our data provide the basis for determining the three-dimensional solution structures of these proteins and characterizing their immunological cross-reactivity on a structural basis. NMR resonance assignments of the PR-10 allergens Act c 8 and Act d 8 from golden and green kiwifruit.,Zeindl R, Tollinger M Biomol NMR Assign. 2021 Oct;15(2):367-371. doi: 10.1007/s12104-021-10031-w. Epub , 2021 Jun 9. PMID:34106433[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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