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

Food Chem. 2016 Nov 1;210:70-7. doi: 10.1016/j.foodchem.2016.04.068. Epub 2016 Apr 20.


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.

Keywords: Albumin; Basophil activation test; Pin p 1; Pine nut allergy; Tree nut allergy.

MeSH terms

  • 2S Albumins, Plant / genetics*
  • 2S Albumins, Plant / metabolism
  • Albumins / genetics*
  • Albumins / metabolism
  • Allergens / genetics*
  • Allergens / metabolism
  • Basophils
  • Cycadopsida
  • Humans
  • Immunoglobulin E / metabolism
  • Nuts / genetics*
  • Nuts / metabolism
  • Phylogeny
  • Plant Proteins / genetics*
  • Plant Proteins / metabolism


  • 2S Albumins, Plant
  • Albumins
  • Allergens
  • Plant Proteins
  • Immunoglobulin E