Abstract: A method of making and a modified allergen having reduced allergenicity and preserved immunogenicity compared to corresponding native allergenic material. The preserved immunogenicity is elicited by a IgG-mediated antibody response, all or part of the primary amine groups of the lysine residues of the native allergenic material are functionalized with carbamoyl or thiocarbamoyl moieties, and all or part of the primary amine groups of the arginine residues of the carbamoyl- or thiocarbamoyl functionalized allergenic material are further functionalized with dialdehyde or diketal moieties. The raw allergenic material is selected from the group consisting of DP mites extract, Der p1, ovalbumin and Lipid Transfer Protein (LTP), the average percentage of modified primary amine groups of the lysine ranges between 75% and 100%; and the average percentage of the substituted arginine residues ranges between 25% and 10%.

Abstract: A method of making and a modified allergen having reduced allergenicity and preserved immunogenicity compared to corresponding native allergenic material. The preserved immunogenicity is elicited by a IgG-mediated antibody response, all or part of the primary amine groups of the lysine residues of the native allergenic material are functionalized with carbamoyl or thiocarbamoyl moieties, and all or part of the primary amine groups of the arginine residues of the carbamoyl- or thiocarbamoyl functionalized allergenic material are further functionalized with dialdehyde or diketal moieties. The raw allergenic material is selected from the group consisting of DP mites extract, Der p1, ovalbumin and Lipid Transfer Protein (LTP), the average percentage of modified primary amine groups of the lysine ranges between 75% and 100%; and the average percentage of the substituted arginine residues ranges between 25% and 10%.

Abstract: The present invention concerns the preparation of purified allergens and allergoids, both derived from whole bee venom, for the desensitization (immunotherapy) of subjects affected by a specific allergy. In particular, the present invention concerns a preparation for immunotherapy based on purified bee venom, characterized in that said bee venom is essentially mellitin-free. In addition, the preparation of a monomeric allergoid obtainable through the carbamylation or thiocarbamylation reaction of said mellitin-free bee venom, is described. Said allergoid, being characterized by reduced IgE-binding activity, may be a safer and more effective candidate for specific immunotherapy.

Abstract: Modified allergens having reduced allergenicity compared to corresponding native allergenic material, wherein all or a part of the primary amine groups of the lysine and arginine residues of the allergenic molecules are functionalized and the modified allergens have the structure wherein R and R2 are independently selected from H, C1-C5 alkyl, phenyl, phenyl substituted in ortho, meta, or para with a hydroxy, C1-C4 alkoxy, halogen, amino, alkylamino, dialkylamino, mercapto, C1-C4 alkylmercapto group; X represents O, S, or NR3, where R3 is H, alkyl with 1-6 carbon atoms, phenyl, or CN; R1 represents H, alkyl with 1-8 carbon atoms, phenyl or arylalkyl with up to 8 carbon atoms, or alkyl containing a heterocyclic ring; prot represents the protein residue of the allergen; n is the number of functionalized arginine groups and ranges between 1 and the number of arginine groups present in the allergen; m is the number of functionalized lysine groups and ranges between 1 and the number of lysine groups present in

Abstract: The present invention concerns the preparation of purified allergens and allergoids, both derived from whole bee venom, for the desensitisation (immunotherapy) of subjects affected by a specific allergy. In particular, the present invention concerns a preparation for immunotherapy based on purified bee venom, characterised in that said bee venom is essentially mellitin-free. In addition, the preparation of a monomeric allergoid obtainable through the carbamylation or thiocarbamylation reaction of said mellitin-free bee venom, is described. Said allergoid, being characterised by reduced IgE-binding activity, may be a safer and more effective candidate for specific immunotherapy.