The present invention provides anti-HLA-DQ2.5 antibodies. The anti-HLA-DQ2.5 antibodies of the invention have binding activity to complexes formed by HLA-DQ2.5 and a gluten peptide, but have substantially no binding activity to complexes formed by HL A-DQ2.5 and an irrelevant peptide. Furthermore, it was found that the antibodies of the invention have inhibitory effects on T cell activation.

The invention generally relates to therapeutic compositions and methods for treating and suppressing allergic responses.

The invention generally relates to therapeutic compositions and methods for treating and suppressing allergic responses.

The present invention provides anti-gliadin antibodies and antibody fragments, and polypeptides encoding the antibodies or fragment. Also disclosed are methods and Kits for the use of such antibodies, fragments, or polypeptides in detection of gliadin. Further provided are heavy chain and light chain variable sequences and associated sequences of complementarity-determining regions (CDRs).

The present invention provides anti-gliadin antibodies and antibody fragments, and polypeptides encoding the antibodies or fragment. Also disclosed are methods and Kits for the use of such antibodies, fragments, or polypeptides in detection of gliadin. Further provided are heavy chain and light chain variable sequences and associated sequences of complementarity-determining regions (CDRs).

Provided herein are antibodies that bind Fagales allergens, Fagales related allergens, birch pollen, or Bet v 1, compositions comprising the antibodies, nucleic acids encoding the antibodies, and methods of using the antibodies. According to certain embodiments, the antibodies are fully human monoclonal antibodies that bind to Bet v 1. The antibodies are useful for binding Bet v 1 in vivo, thus preventing binding of the allergen to pre-formed IgE on the surface of mast cells or basophils. In doing so, the antibodies act to prevent the release of histamine and other inflammatory mediators from mast cells and/or basophils, thus ameliorating the untoward response to the Fagales allergens in sensitized individuals.

Provided herein are antibodies that bind Fagales allergens, Fagales related allergens, birch pollen, or Bet v 1, compositions comprising the antibodies, nucleic acids encoding the antibodies, and methods of using the antibodies. According to certain embodiments, the antibodies are fully human monoclonal antibodies that bind to Bet v 1. The antibodies are useful for binding Bet v 1 in vivo, thus preventing binding of the allergen to pre-formed IgE on the surface of mast cells or basophils. In doing so, the antibodies act to prevent the release of histamine and other inflammatory mediators from mast cells and/or basophils, thus ameliorating the untoward response to the Fagales allergens in sensitized individuals.

The inventors has developed a recombinant molecular system, named OptoFab, allowing the accurate control of the agonistic properties of an antibody-derived Fab fragment in time and in space using specific wavelengths of light. It consists in a Fab fragment derived from an agonistic antibody of interest, linked to optogenetic modules that confer a light response capacity. Indeed, antibody derived Fab fragments generally keep the specificity of the antibody for its epitope, but not its agonistic properties. However, when Fab fragments are oligomerized, they recover the agonistic properties of the whole antibody. These characteristics, are at the basis of the OptoFab concept as its objective is to manipulate the oligomerization/immobilization statue of a Fab fragment using optogenetics to control its agonistic property. The present invention relates to methods and systems for controlling the agonistic properties of antibody variable domains by light.

The inventors has developed a recombinant molecular system, named OptoFab, allowing the accurate control of the agonistic properties of an antibody-derived Fab fragment in time and in space using specific wavelengths of light. It consists in a Fab fragment derived from an agonistic antibody of interest, linked to optogenetic modules that confer a light response capacity. Indeed, antibody derived Fab fragments generally keep the specificity of the antibody for its epitope, but not its agonistic properties. However, when Fab fragments are oligomerized, they recover the agonistic properties of the whole antibody. These characteristics, are at the basis of the OptoFab concept as its objective is to manipulate the oligomerization/immobilization statue of a Fab fragment using optogenetics to control its agonistic property. The present invention relates to methods and systems for controlling the agonistic properties of antibody variable domains by light.

The present disclosure provides methods for treating, preventing, or ameliorating one or more symptoms of birch allergy or allergic disease in a subject by administering to the subject an antibody or antigen-binding fragment thereof that binds Bet v 1, or a cocktail of antibodies or antigen-binding fragments thereof that bind Bet v 1.