The network aims at generating recombinant allergens and modified recombinant allergens based on structural allergology for industrial production of test vaccines against Age-mediated allergy. Specific allergy vaccination (immunotherapy) is the only therapeutic treatment available that changes the natural course of the allergic disease and has the potential to be preventive. Today's vaccines are derived from natural source. Vaccines based on recombinant allergens will provide vaccines with increased safety profile and clinical efficacy.
In summary, the lack of recombinant Ves v 1 and Der p 1 has been major obstacles in the developing and testing of complete recombinant vaccins towards wasp and house-dust mites, respectively. Activities addressing this issue is continuing outside the TRAFSA project. The future recombinant active ingredient of a vaccine against cat allergy has been isolated and characterised, forming the basis for further pre-clinical work. Wasp venom vaccine. A complete recombinant wasp vaccine should consist of three components; Ves v 1, Ves v 2 and Ves v 5. Ves v 1. This protein has proven to be difficult to express in its recombinant form, hampering any immunochemical and/or biological charaterisation. Ves v 2. This component has been successfully expressed, purified and charaterised. The crystal structure was solved and human epitopes mapped. Ves v 5. This component was partially charaterised prior to the project and has been further tested and epitope mapped. An animal model for tolerance induction was developed within the project. Cat allergy vaccine.

The major component of a future recombinant cat vaccine, Fel d 1, has been successfully expressed and characterised. The recombinant molecule is indistinguishable from its natural counterpart in terms of structure and immunological activity. House-dust mite allergy vaccine. The recombinant vaccine should consist of two components; Der p 1 and Der p 2. Der p 1. This component has also shown to be difficult to express in the systems tried during the project, hampering a detailed characterisation of the molecule. Der p 2. This component has been sucessfully expressed and characterised. An analog, Der f 2, has been crystallised and its structure solved, revealing cross-reactive allergic epitopes shared between Der p 2 and Der f 2. Immune responses towards natural Der p 1 and Der p 2 have been studied in animal models and mutants of Der p 2 have been designed.