Author: Kopertekh, Lilya; Meyer, Torsten; Freyer, Cornelia; Hust, Michael
Title: Transient plant production of Salmonella Typhimurium diagnostic antibodies Document date: 2019_2_12
ID: y47ahl3p_30
Snippet: The functionality of plant-derived antibody fragments was determined by ELISA. To this end ELISA plates were coated with OmpD recombinant protein and probed with different dilutions of purified antibody fragments. As shown in Fig. 6a plant-produced antibodies were able to recognize the OmpD antigen. The binding to OmpD protein increased with the concentration of scFv-TM43-E10 and scFv-Fc-TM43-E10 proteins in the reaction. The antigen binding acti.....
Document: The functionality of plant-derived antibody fragments was determined by ELISA. To this end ELISA plates were coated with OmpD recombinant protein and probed with different dilutions of purified antibody fragments. As shown in Fig. 6a plant-produced antibodies were able to recognize the OmpD antigen. The binding to OmpD protein increased with the concentration of scFv-TM43-E10 and scFv-Fc-TM43-E10 proteins in the reaction. The antigen binding activity of plant-derived antibodies was further compared with the scFv-TM43-E10 produced in bacterial cells. The scFv-Fc-TM43-E10 format extracted from mammalian cell culture served as a reference for the scFv-Fc derivative isolated from plant tissue. As expected the scFv-TM43-E10 preparations from both plant material and bacterial cells exhibited similar binding properties. The sensitivity of scFv-Fc-TM43-E10 plantibody to OmpD was also comparable to that of the scFv-Fc format generated in mammalian cells.
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