원문정보
초록
영어
Plant genetic engineering has led to production of plant-derived mAb (mAbP), which provides an inexpensive, efficient and safe alternative to traditional systems used for the production of recombinant antibodies. In this study, the expression levels of mAbP SO57 with or without ER-retention signal peptide (Lys-Asp-Glu-Leu; KDEL) in transgenic tobacco plants were analyzed. The expression levels of mAbP SO57 with KDEL were significantly higher than those in the without KDEL regardless of transcription level. Localization of mAbP SO57 with KDEL in the perinuclear region suggests that the mAbP with KDEL is localized in the ER. The mAbP without KDEL and mAbH had mainly Golgi type glycans, whereas the ER-localized mAbP with KDEL contained both oligomannose (47.6%) and Golgi type glycans (52.4%). The Fc domains of both purified mAbP (with and without KDEL) and human-derived mAb (mAbH) had similar binding activity to the FcγRI receptor (CD64). Both mAbP (with and without KDEL) had a shorter half-life than mAbH. However, both mAbP with and without KDEL were as effective at neutralizing activity of the rabies virus CVS-11 as the mAbH. These results suggest that the ER localization of a recombinant mAbP with a C-terminal KDEL sequence induces the reprogramming of glycosylation pathways and the enhancement of functional antiviral therapeutic antibody production in the plants.