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.
Highlights
In the northern hemisphere, individuals who are sensitized to birch pollen show IgE serum reactivity against the protein Bet v 1, the major birch pollen allergen, in about 90% of all cases (Ipsen and Lowenstein 1983; Moverare et al 2002)
Patients suffering from birch pollinosis can develop allergies to fruits and nuts due to immunological cross-reactivity of Bet v 1 specific antibodies to proteins that are present in these kinds of food
Immunological cross-reactivity to birch pollen is related to the protein Pru p 1 that is present in peaches (Mills and Shewry 2004)
Summary
Individuals who are sensitized to birch pollen show IgE serum reactivity against the protein Bet v 1, the major birch pollen allergen, in about 90% of all cases (Ipsen and Lowenstein 1983; Moverare et al 2002). Patients suffering from birch pollinosis can develop allergies to fruits and nuts due to immunological cross-reactivity of Bet v 1 specific antibodies to proteins that are present in these kinds of food. Immunological cross-reactivity to birch pollen is related to the protein Pru p 1 that is present in peaches (Mills and Shewry 2004). We present the solution NMR backbone and side-chain assignment of the recombinantly expressed isoform Pru p 1.0101. This particular isoform shares sequence identity of 59% with the sensitizing allergen Bet v 1.0101 (Gajhede et al 1996). Sequence identity to the most prominent cross-reactive allergen in food, the major allergen from apple (Malus domestica) Mal d 1.0101, is considerably higher (82%) (Ahammer et al 2017, 2016)
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