Worldwide more than 200 million individuals are allergic to group 1 grass pollen
allergens. We have used the major timothy grass pollen
allergen Phl p 1, which cross-reacts with most grass-, corn-, and monocot-derived group 1
allergens to develop a generally applicable strategy for the production of hypoallergenic
allergy vaccines. On the basis of the experimentally determined
B cell epitopes of Phl p 1, we have synthesized five synthetic
peptides. These
peptides are derived from the major Phl p 1
IgE epitopes and were between 28-32
amino acids long. We demonstrate by nuclear magnetic resonance that the
peptides exhibit no secondary and tertiary structure and accordingly failed to bind
IgE antibodies from grass pollen allergic patients. The five
peptides, as well as an equimolar mixture thereof, lacked allergenic activity as demonstrated by basophil histamine release and skin test experiments in grass pollen allergic patients. When used as immunogens in mice and rabbits, the
peptides induced protective
IgG antibodies, which recognized the complete Phl p 1 wild-type
allergen and group 1
allergens from other grass species. Moreover,
peptide-induced
antibodies inhibited the binding of grass pollen allergic patients
IgE antibodies to the wild-type
allergen. We thus demonstrate that synthetic hypoallergenic
peptides derived from
B cell epitopes of major
allergens represent safe
vaccine candidates for the treatment of
IgE- mediated
allergies.