Nature Biotechnology
- 24, 1591 - 1597 (2006)
Published online: 26 November 2006; | doi:10.1038/nbt1260
Glycan optimization of a human monoclonal antibody in the aquatic plant Lemna minorKevin M Cox1, Jason D Sterling1, Jeffrey T Regan1, John R Gasdaska1, Karen K Frantz1, Charles G Peele1, Amelia Black2, David Passmore2, Cristina Moldovan-Loomis2, Mohan Srinivasan2, Severino Cuison2, Pina M Cardarelli2 & Lynn F Dickey11
Biolex Therapeutics, 158 Credle Street, Pittsboro, North Carolina 27312, USA. 2
Medarex, Inc., 521 Cottonwood Drive, Milpitas, California 95035, USA.
Correspondence should be addressed to Kevin M Cox kcox@biolex.com
N-glycosylation is critical to the function of monoclonal antibodies (mAbs) and distinguishes various systems used for their production. We expressed human mAbs in the small aquatic plant Lemna minor, which offers several advantages for manufacturing therapeutic proteins free of zoonotic pathogens1. Glycosylation of a mAb against human CD30 was optimized by co-expressing the heavy and light chains of the mAb with an RNA interference construct targeting expression of the endogenous  -1,3-fucosyltransferase and  -1,2-xylosyltransferase genes. The resultant mAbs contained a single major N-glycan species without detectable plant-specific N-glycans and had better antibody-dependent cell-mediated cytotoxicity and effector cell receptor binding activities than mAbs expressed in cultured Chinese hamster ovary (CHO) cells.
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