Abstract: A method of making an antibody in plants that binds to ricin B chain is described. The method comprises (a) introducing a nucleic acid molecule encoding a heavy chain variable region of the antibody and a nucleic acid molecule encoding a light chain variable region of the antibody into a plant or plant cell; and (b) growing the plant or plant cell to obtain a plant that expresses the antibody or antibody fragment. The disclosure also relates to anti-ricin B chain antibodies and antibody fragments as well as methods of using same in therapy and prophylaxis.

Abstract: A method of making an antibody in plants that binds to ricin is described. The method comprises (a) introducing a nucleic acid molecule encoding a heavy chain variable region of the antibody and a nucleic acid molecule encoding a light chain variable region of the antibody into a plant or plant cell; and (b) growing the plant or plant cell to obtain a plant that expresses the antibody or antibody fragment. The disclosure also relates to anti-ricin antibodies and antibodies fragments as well as methods of using same in therapy and prophylaxis.

Abstract: Expression vectors and methods of their use for enhancing the production of recombinant proteins in plants or plant cells are described. Production can be further enhanced upon co-expression of the P19 suppressor of gene-silencing from tomato bushy stunt virus. Preferably, the recombinant proteins are therapeutic enzymes and/or antibodies and methods are carried out in Nicotiana benthamiana—optionally an RNAi-based glycomodified strain—or in the Nicotiana tabacum cultivar Little Crittenden.

Abstract: The present disclosure relates to methods and uses of improving the therapeutic efficacy and utility of antibody fragments by employing anti-epitope-tagging technologies.

Abstract: A method of making an antibody in plants that binds to a HER receptor is described. The antibody preferably contains sequences from trastuzumab that have been optimized for expression in plants.

Abstract: A method of constructing a VHH library from an immunized camelid, using whole venom or an extract thereof. There is also provided VHH antibody fragments isolated from a library produced in hyperimmunized llama. These VHH antibody fragments were sequenced, and specifically bind ?-cobratoxin.

Abstract: Expression vectors and methods of their use for enhancing the production of recombinant proteins in plants or plant cells are described. Production can be further enhanced upon co-expression of the P19 suppressor of gene-silencing from tomato bushy stunt virus. Preferably, the recombinant proteins are therapeutic enzymes and/or antibodies and methods are carried out in Nicotiana benthamiana—optionally an RNAi-based glycomodified strain—or in the Nicotiana tabacum cultivar Little Crittenden.

Abstract: The present disclosure relates to methods and uses of improving the therapeutic efficacy and utility of antibody fragments by employing anti-epitope-tagging technologies.

Abstract: A method of constructing a VHH library from an immunized camelid, using whole venom or an extract thereof. There is also provided VHH antibody fragments isolated from a library produced in hyperimmunized llama. These VHH antibody fragments were sequenced, and specifically bind to ?-cobratoxin.

Abstract: A method of constructing a VHH library from an immunized camelid, using whole venom or an extract thereof There is also provided VHH antibody fragments isolated from a library produced in hyperimmunized llama These VHH antibody fragments were sequenced, and specifically bind ?-cobratoxin.

Abstract: A method of making an antibody in plants that binds to a HER receptor is described. The antibody preferably contains sequences from trastuzumab that have been optimized for expression in plants.

Abstract: A method of constructing a VHH library from an immunized camelid, using whole venom or an extract thereof There is also provided VHH antibody fragments isolated from a library produced in hyperimmunized llama These VHH antibody fragments were sequenced, and specifically bind ?-cobratoxin.