Interacelluar reprogramming of expression, glycosylation, and function of plant-derived anti-virus therapeutic monoclonal antibody

다국어 초록 (Multilingual Abstract)

Plant genetic engineering has led to production of plant-derived mAb (mAbP), which can provides a safe and economically effective alternative to the conventional antibody expression methods. In this study, the expression levels of mAbP SO57 with or without ER-retention peptide extensions signal (Lys-Asp-Glu-Leu; KDEL) in transgenic tobacco plants were analysed in transgenic plant. The expression levels of mAbP SO57 with KDEL were significantly higher than that without KDEL regardless of transcription level. mAbP SO57 with KDEL localized surround to the nucleus suggesting that the mAbP with KDEL is localized in ER. The mAbP without KDEL and mAbH had mainly Golgi type glycans, whereas the ER-localized mAbP with KDEL had glycan profile with both oligomannose type (47.6%) and Golgi type (52.4%). The Fc domains of both purified mAbP (with and without KDEL) and human-derived mAb (mAbH) had similar bingding activity to the Fcγ RI receptor (CD64). Both mAbP (with and without KDEL) had a shorter half-life than mAbH. However, both mAbP with and without KDEL was as effective at neutralizing activity of the rabies virus CVS-11 as the mAbH. These results suggest that ER localization of recombinant mAbP by KDEL reprograms glycosylation and enhances production of the functional antivirus therapeutic antibody in the plant.