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- Title
Optimization of humanized IgGs in glycoengineered Pichia pastoris.
- Authors
Huijuan Li; Sethuraman, Natarajan; Stadheim, Terrance A.; Zha, Dongxing; Prinz, Bianka; Ballew, Nicole; Bobrowicz, Piotr; Choi, Byung-Kwon; Cook, W. James; Cukan, Michael; Houston-Cummings, Nga Rewa; Davidson, Robert; Gong, Bing; Hamilton, Stephen R.; Hoopes, Jack P.; Jiang, Youwei; Kim, Nam; Mansfield, Renee; Nett, Juergen H.; Rios, Sandra
- Abstract
As the fastest growing class of therapeutic proteins, monoclonal antibodies (mAbs) represent a major potential drug class. Human antibodies are glycosylated in their native state and all clinically approved mAbs are produced by mammalian cell lines, which secrete mAbs with glycosylation structures that are similar, but not identical, to their human counterparts. Glycosylation of mAbs influences their interaction with immune effector cells that kill antibody-targeted cells. Here we demonstrate that human antibodies with specific human N-glycan structures can be produced in glycoengineered lines of the yeast Pichia pastoris and that antibody-mediated effector functions can be optimized by generating specific glycoforms. Glycoengineered P. pastoris provides a general platform for producing recombinant antibodies with human N-glycosylation.
- Publication
Nature Biotechnology, 2006, Vol 24, Issue 2, p210
- ISSN
1087-0156
- Publication type
Academic Journal
- DOI
10.1038/nbt1178