title: Identification of a plane pollen lipid transfer protein (Pla a 3) and its immunological relation to the peach lipid-transfer protein, Pru p 3.
abstract: BACKGROUND
  An association between plane tree pollen allergy and plant food allergy has been described, but the cross-reacting allergens have not yet been identified. The aim of this study was the identification of homologous non-specific lipid-transfer proteins (nsLTPs) in plane pollen, and to investigate its immunological relationship with the peach LTP, Pru p 3.
  
  
  METHODS
  Three different patient groups were recruited in Spain: 22 plane pollen-allergic patients without food allergy (A), 36 plane pollen-allergic patients with peach allergy (B) and 10 peach-allergic patients without plane pollen allergy (C). Proteins from plane pollen extract were fractionated by ion-exchange and reversed-phase chromatography. Further methods applied were N-terminal amino acid sequence analysis, immunoblotting, enzyme allergosorbent test, CAP and basophil histamine release assays.
  
  
  RESULTS
  A 10 kDa IgE-reactive protein was purified from plane pollen and identified as nsLTP. Pla a 3 was characterized as a minor allergen (27.3%) in plane pollen-allergic patients without food allergy (A) and as a major allergen in plane pollen-allergic patients with peach allergy (B) showing a prevalence of IgE-reactivity of 63.8%. Group B contained patients sensitized to Pru p 3 without IgE-reactivity to plane-LTP (16.6%). By contrast, Pla a 3 IgE-reactive patients without sensitization to Pru p 3 could be found (16.6%). The sera of patients sensitized to both LTPs (50%), Pla a 3 and Pru p 3, showed different biological activity in histamine release assay: depending on individual patient's sera tested, Pla a 3 showed a similar, a stronger or a weaker allergenic potency in comparison with Pru p 3.
  
  
  CONCLUSIONS
  Plane LTP is a major allergen in plane pollen-allergic patients with peach allergy recruited in the Mediterranean area. The results of histamine release tests and different IgE-binding profiles pointed towards the existence of species-specific IgE epitopes. Likewise, no general conclusion on the sensitizer could be made.
authors.affiliation: Department of Allergology, Paul-Ehrlich-Institut, Langen, Germany. lauir@pei.de
authors.forename: I
authors.initials: I
authors.lastname: Lauer
authors.forename: M S
authors.initials: MS
authors.lastname: Miguel-Moncin
authors.forename: T
authors.initials: T
authors.lastname: Abel
authors.forename: K
authors.initials: K
authors.lastname: Foetisch
authors.forename: C
authors.initials: C
authors.lastname: Hartz
authors.forename: D
authors.initials: D
authors.lastname: Fortunato
authors.forename: A
authors.initials: A
authors.lastname: Cistero-Bahima
authors.forename: S
authors.initials: S
authors.lastname: Vieths
authors.forename: S
authors.initials: S
authors.lastname: Scheurer
mesh_terms: D000485:Allergens; D052179:Antigens, Plant / Q000032:analysis / Q000276:immunology*; D002352:Carrier Proteins / Q000032:analysis / Q000276:immunology*; D003429:Cross Reactions; D005512:Food Hypersensitivity / Q000276:immunology*; D006801:Humans; D010940:Plant Proteins / Q000032:analysis / Q000276:immunology*; D027861:Prunus / Q000276:immunology*; D006255:Rhinitis, Allergic, Seasonal / Q000276:immunology*; D014197:Trees / Q000276:immunology*
chemical_list: D000485:Allergens; D052179:Antigens, Plant; D002352:Carrier Proteins; D010940:Plant Proteins; C511920:lipid transfer proteins, plant