title: Comparison of IgE-binding capacity, cross-reactivity and biological potency of allergenic non-specific lipid transfer proteins from peach, cherry and hazelnut.
abstract: BACKGROUND
  Whether the observed clinical pattern of non-specific lipid transfer protein (nsLTP)-mediated food allergies is attributable to a primary sensitization by Pru p 3 from peach and subsequent cross-reactivity with Rosaceae- and non-Rosaceae-derived foods expressing homologous allergens is still unclear.
  
  
  OBJECTIVE
  To investigate the allergenic properties of nsLTPs from Rosaceae and non-Rosaceae foods.
  
  
  METHODS
  In peach-, cherry- or hazelnut-allergic patients, prevalence of sensitization, IgE-binding capacity, cross-reactivity and allergenic potency of Pru p 3 was compared with Pru av 3 (cherry) and Cor a 8 (hazelnut).
  
  
  RESULTS
  Frequency of sensitization to corresponding nsLTPs was 88, 85, and 77% in peach-, hazelnut- and cherry-allergic patients, respectively. Concomitant allergic reactions to cherry and hazelnut were reported in 51 and 44% of peach-allergic patients, respectively. In contrast to cherry allergy, hazelnut allergy was not strictly associated to peach allergy. Sensitization to Cor a 8 or Pru av 3 was strongly correlated with IgE reactivity to Pru p 3, even when subjects tolerated peach. Specific IgE was highest for Rosaceae LTPs, and cross-inhibition experiments confirmed a stronger IgE-binding capacity of Pru p 3 than Cor a 8. The biological potency of Pru p 3 and Pru av 3 was similar but stronger for both nsLTPs than that of Cor a 8.
  
  
  CONCLUSIONS
  Clinical cross-reactivity of food-allergic patients in the Mediterranean area is likely attributed to a primary sensitization to Pru p 3 and serological cross-reactivity with homologous food nsLTPs. In comparison to Cor a 8, Rosaceae nsLTPs showed a stronger IgE-binding capacity and allergenic potency indicating a different epitope pattern.
authors.affiliation: Division of Allergology, Paul-Ehrlich-Institute, Langen, Germany.
authors.forename: Christina
authors.initials: C
authors.lastname: Hartz
authors.forename: Iris
authors.initials: I
authors.lastname: Lauer
authors.forename: Maria
authors.initials: M
authors.lastname: del Mar San Miguel Moncin
authors.forename: Anna
authors.initials: A
authors.lastname: Cistero-Bahima
authors.forename: Kay
authors.initials: K
authors.lastname: Foetisch
authors.forename: Jonas
authors.initials: J
authors.lastname: Lidholm
authors.forename: Stefan
authors.initials: S
authors.lastname: Vieths
authors.forename: Stephan
authors.initials: S
authors.lastname: Scheurer
mesh_terms: D000293:Adolescent; D000328:Adult; D000485:Allergens / Q000276:immunology* / Q000378:metabolism; D052179:Antigens, Plant / Q000276:immunology / Q000378:metabolism; D002352:Carrier Proteins / Q000276:immunology / Q000378:metabolism; D002648:Child; D031211:Corylus; D003429:Cross Reactions / Q000276:immunology; D005260:Female; D005512:Food Hypersensitivity / Q000453:epidemiology / Q000276:immunology*; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology / Q000378:metabolism*; D008297:Male; D019083:Mediterranean Region; D010940:Plant Proteins / Q000276:immunology / Q000378:metabolism; D015995:Prevalence; D011485:Protein Binding; D027861:Prunus; D027824:Rosaceae
chemical_list: D000485:Allergens; D052179:Antigens, Plant; D002352:Carrier Proteins; C527352:Cor a 8 allergen, Corylus avellana; D010940:Plant Proteins; C514372:Pru av 3 allergen, Prunus avium; C463181:Pru p 3 allergen; C511920:lipid transfer proteins, plant; D007073:Immunoglobulin E