Abstract：
:In Europe, Northern America, and China a large number of individuals are suffering from peach (Prunus persica) allergy caused by the protein Pru p 1. Immunologic reactions against this 17.5 kDa protein result from initial sensitization to the birch (Betula verrucosa) pollen allergen Bet v 1 and subsequent immunologic cross-reactivity of Bet v 1 specific antibodies. Allergic symptoms typically include severe itching, scratching of the throat, and rhino conjunctivitis. So far, experimental structural data for the peach allergen Pru p 1 are not available. In a first step towards the elucidation of the structure of this protein we assigned backbone and side chain 1H, 13C, and 15N chemical shifts of the naturally occurring isoform Pru p 1.0101 by solution NMR spectroscopy. Our chemical shift data indicate that this protein fold consists of seven β-strands separated by two short α-helices and a long C-terminal α-helix, which is in accordance with the reported crystal structure of Bet v 1. Our data provide the basis for determining the three-dimensional solution structure of this protein and to characterize its immunologic cross-reactivity on a structural basis.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Führer S,Trimmel S,Breuker K,Tollinger Mdoi
10.1007/s12104-018-9864-xsubject
Has Abstractpub_date
2019-04-01 00:00:00pages
127-130issue
1eissn
1874-2718issn
1874-270Xpii
10.1007/s12104-018-9864-xjournal_volume
13pub_type
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journal_title：Biomolecular NMR assignments
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journal_title：Biomolecular NMR assignments
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