Allergenicity and antigenicity of wild-type and mutant, monomeric, and dimeric carrot major allergen Dau c 1: Destruction of conformation, not oligomerization, is the roadmap to save allergen vaccines

Comparison of secondary structures by CD dichroism spectrometry: comparison of monomeric wild-type and mutant Dau c 1.01 and Dau c 1.02 (A); comparison of wild-type and mutant dimer (B); comparison of wild-type Dau c 1.01 monomer and trimer (C).

Titration of murine IgG antibody responses by ELISA. Immunogen and doses are given in the title of each subfigure (A-H). The explanation for the symbols representing the test antigens in the ELISA is given in B for all subfigures.

Correlation analysis of IgE antibody reactivities among monomeric and oligomeric, natural, and mutated Dau c 1 isoforms (A-D). One serum had a very high IgE antibody response (specific IgE > 50 IU/mL) to wild-type Dau c 1 forms and was not shown in this figure. This serum, however, was included for statistical and linear regression analysis.

Histamine release from peripheral basophils of 2 subjects with carrot allergy, PEI 61 (A) and PEI 62 (B), and a control subject without allergy, PEI 232 (C), after stimulation with carrot extract, Dau c 1.01 and Dau c 1.02 wild-type and mutant monomers and dimers, and Dau c 1.01 trimer.

Inhibition of human IgE antibody reactivities to Dau c 1.01 (A) or Dau c 1.02 (B) by murine serum pools. Mice were immunized with mixtures of wild-type and mutant Dau c 1.01 and Dau c 1.02 as well as the corresponding dimers.