Reduction of IgE antibody binding to rDer p 2 variants generated by site-directed mutagenesis.

Abstract

Our studies have focused on the 14 kD Group 2 allergens of D. pteronyssinus which are potent immunogens and elicit humoral and cellular responses in 80–90% of mite allergic individuals. Previous studies have shown that the B cell epitopes are heat and pH resistant, but are destroyed upon reduction and alkylation, suggesting that these determinants are dependent on the tertiary structure of the protein (1). This conclusion is supported by studies that showed a low prevalence of IgE Ab binding to polypeptide fragments produced from truncated Der p 2 cDNA (2,3).Synthetic peptides spanning the entire Der p 2 sequence have also been used to map Ab binding regions, however, only one peptide, amino acids 65–78, retained IgE Ab binding, confirming that the majority of epitopes are conformational (4). Taken together, these studies suggested that an alternative approach was required to further map the conformational determinants on Group 2 allergens.KeywordsAtopic DermatitisCell EpitopeSurface ResidueInhibition CurveIntradermal Skin TestingThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.