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CUTTING EDGE |
*
DIBIT, San Raffaele Scientific Institute, Milan, Italy;
Roche Milano Ricerche, Milan, Italy;
Roche Discovery Technologies, Hoffmann-La Roche, Nutley, NJ 07110; and
§
Science Park, San Raffaele Scientific Institute, Milan, Italy
Although atopic allergy affects 
20% of the total population,
the relationship between the protein structure and immunogenic activity
of the allergens is still largely unknown. We observed that group 5
grass allergens are characterized by repeated structural motifs. Using
a new algorithm, TEPITOPE, we predicted promiscuous HLA-DR ligands
within the repeated motifs of the Lol p5a allergen from
rye grass. In vitro binding studies confirmed the promiscuous binding
characteristics of these peptides. Moreover, most of the predicted
ligands were novel T cell epitopes that were able to stimulate T
cells from atopic patients. We generated a panel of Lol
p5a-specific T cell clones, the majority of which recognized
the peptides in a cross-reactive fashion. The computational prediction
of DR ligands might thus allow the design of T cell epitopes with
potential useful application in novel immunotherapy
strategies.
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