title: Relevance of IgE binding to short peptides for the allergenic activity of food allergens.
abstract: BACKGROUND
  Analysis of IgE antibody binding to epitopes provides information for food allergy diagnosis and management and construction of hypoallergenic candidate vaccines, but the contribution of sequential epitopes to functionally relevant IgE binding is not fully understood.
  
  
  OBJECTIVE
  We sought to study the impact of IgE-binding peptides described as major sequence epitopes in the literature on IgE-binding capacity of 2 selected food allergens.
  
  
  METHODS
  IgE-binding peptides of the food allergens Ara h 2 (peanut) and Pen a 1 (shrimp) were identified. Synthetic soluble peptides representing the identified sequences were assessed for their capacity to inhibit IgE binding to the parent allergens by means of ELISA and in mediator release assay. The IgE-binding capacity of unfolded recombinant (r) Ara h 2 was analyzed. A hybrid tropomyosin carrying the IgE-binding regions of Pen a 1 grafted into the structural context of the nonallergenic mouse tropomyosin was applied in ELISA inhibition experiments and ImmunoCAP analysis.
  
  
  RESULTS
  Although IgE-binding peptides representing sections of the allergen sequences were detected, no relevant capacity to inhibit the IgE binding to the parent allergen in ELISA or basophil activation test was observed. Unfolded rAra h 2 showed reduced IgE-binding capacity compared with folded rAra h 2 and failed to elicit mediator release. Hybrid tropomyosin bound less IgE than rPen a 1 in ImmunoCAP analysis and revealed marginal inhibitory capacity.
  
  
  CONCLUSIONS
  Peptides identified as major sequence epitopes on Pen a 1 and Ara h 2 show little contribution to the IgE binding of the allergens studied.
authors: Division of Allergology, Paul-Ehrlich-Institut, Langen, Germany.
authors: Melanie
authors: M
authors: Albrecht
authors: Yvonne
authors: Y
authors: Kühne
authors: Barbara K
authors: BK
authors: Ballmer-Weber
authors: Wolf-Meinhard
authors: WM
authors: Becker
authors: Thomas
authors: T
authors: Holzhauser
authors: Iris
authors: I
authors: Lauer
authors: Andreas
authors: A
authors: Reuter
authors: Stefanie
authors: S
authors: Randow
authors: Sabine
authors: S
authors: Falk
authors: Andrea
authors: A
authors: Wangorsch
authors: Jonas
authors: J
authors: Lidholm
authors: Gerald
authors: G
authors: Reese
authors: Stefan
authors: S
authors: Vieths
mesh_terms: D055516:2S Albumins, Plant / Q000276:immunology*; D000485:Allergens / Q000276:immunology*; D000818:Animals; D052179:Antigens, Plant; D018604:Epitope Mapping; D000939:Epitopes / Q000276:immunology; D005512:Food Hypersensitivity / Q000276:immunology*; D006023:Glycoproteins / Q000276:immunology*; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology*; D051379:Mice; D010446:Peptide Fragments / Q000276:immunology; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000276:immunology; D014335:Tropomyosin / Q000276:immunology / Q000378:metabolism; D014612:Vaccines / Q000276:immunology
chemical_list: D055516:2S Albumins, Plant; D000485:Allergens; D052179:Antigens, Plant; C500890:Ara h 2 allergen, Arachis hypogaea; D000939:Epitopes; D006023:Glycoproteins; C513564:Pen a 1 allergen, Penaeus aztecus; D010446:Peptide Fragments; D011994:Recombinant Proteins; D014335:Tropomyosin; D014612:Vaccines; D007073:Immunoglobulin E