Nature Biotechnology 24, 210 - 215 (2006)
Published online: 22 January 2006; | doi:10.1038/nbt1178
Optimization of humanized IgGs in glycoengineered Pichia pastorisHuijuan Li1, Natarajan Sethuraman1, Terrance A Stadheim1, Dongxing Zha1, Bianka Prinz1, Nicole Ballew1, Piotr Bobrowicz1, Byung-Kwon Choi1, W James Cook1, Michael Cukan1, Nga Rewa Houston-Cummings1, Robert Davidson1, Bing Gong1, Stephen R Hamilton1, Jack P Hoopes2, Youwei Jiang1, Nam Kim1, Renee Mansfield1, Juergen H Nett1, Sandra Rios1, Rendall Strawbridge2, Stefan Wildt1
& Tillman U Gerngross31
GlycoFi Inc. 21 Lafayette Street, Lebanon, New Hampshire, 03766, USA. 2
Department of Surgery, Dartmouth-Hitchcock Medical Center, Lebanon, New Hampshire 03766, USA. 3
Thayer School of Engineering, Department of Biological Sciences and the Department of Chemistry, Dartmouth College, Hanover, New Hampshire 03755, USA.
Correspondence should be addressed to Tillman U Gerngross tillman.gerngross@dartmouth.edu As the fastest growing class of therapeutic proteins, monoclonal antibodies (mAbs) represent a major potential drug class1. 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 cells2,
3,
4,
5,
6. 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.
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