NMR resonance assignments of the pathogenesis-related peach allergen Pru p 1.0101.

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 Assign

authors

Führer S,Trimmel S,Breuker K,Tollinger M

doi

10.1007/s12104-018-9864-x

subject

Has Abstract

pub_date

2019-04-01 00:00:00

pages

127-130

issue

1

eissn

1874-2718

issn

1874-270X

pii

10.1007/s12104-018-9864-x

journal_volume

13

pub_type

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