Vicilin allergens of peanut and tree nuts (walnut, hazelnut and cashew nut) share structurally related IgE-binding epitopes

Mol Immunol. 2008 Mar;45(5):1231-40. doi: 10.1016/j.molimm.2007.09.014. Epub 2007 Oct 29.

Abstract

Surface-exposed IgE-binding epitopes of close overall conformation were characterized on the molecular surface of three-dimensional models built for the vicilin allergens of peanut (Ara h 1), walnut (Jug r 2), hazelnut (Cor a 11) and cashew nut (Ana o 1). They correspond to linear stretches of conserved amino acid sequences mainly located along the C-terminus of the polypeptide chains. A glyco-epitope corresponding to an exposed N-glycosylation site could also interfere with the IgE-binding epitopes. All these epitopic regions should participate in the IgE-binding cross-reactivity commonly reported between tree nuts or between peanut and some tree nuts in sensitized individuals. Owing to this epitopic community which constitutes a risk of cross-sensitization, the avoidance or a restricted consumption of other tree nuts should be recommended to peanut-sensitized individuals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anacardium / immunology
  • Arachis
  • Binding Sites
  • Conserved Sequence
  • Corylus / immunology
  • Cross Reactions / immunology
  • Epitopes / metabolism
  • Hypersensitivity
  • Immunoglobulin E / metabolism
  • Juglans / immunology
  • Magnoliopsida / immunology*
  • Nuts / immunology*
  • Plant Proteins / immunology*
  • Seed Storage Proteins

Substances

  • Epitopes
  • Plant Proteins
  • Seed Storage Proteins
  • Immunoglobulin E
  • vicilin protein, plant