Details

Autor(en) / Beteiligte

• Cabanillas, Beatriz
• Crespo, Jesus F.
• Maleki, Soheila J.
• Rodriguez, Julia
• Novak, Natalija

Titel

Pin p 1 is a major allergen in pine nut and the first food allergen described in the plant group of gymnosperms

Ist Teil von

• Food chemistry, 2016-11, Vol.210, p.70-77

Ort / Verlag

England: Elsevier Ltd

Erscheinungsjahr

2016

Quelle

MEDLINE

Beschreibungen/Notizen

• •The 2S albumin Pin p 1 is a major allergen in pine nut.•Pin p 1 sequence showed low homologies with 2S albumins from angiosperms species.•Pin p 1 has a conserved skeleton of 8 cysteines, important for tertiary structure. This study aimed to report the complete sequence of a 2S albumin purified from pine nut and to analyze its allergenic properties. Individual recognition of this protein by serum IgE from pine nut-allergic patients was assessed. IgE cross-linking capacity was analyzed in a basophil activation test. Inhibition of IgE-binding and stability to heating was also assessed. The complete nucleotide sequence was obtained and a phylogenetic study was carried out. 2S albumin from pine nut (registered as Pin p 1.0101) was recognized by IgE of 75% of sera. The allergen was heat-stable and had a robust capacity to inhibit IgE-binding to whole pine nut extract. The IgE cross-linking capacity of Pin p 1 on basophils was also demonstrated. Despite the low homology of Pin p 1 sequence with other allergenic 2S albumins from angiosperms, Pin p 1 contains the typical skeleton of 8 cysteine residues, important for its α-helixes enriched structure.