Optimization of Humanized IgGs in Glycoengineered Pichia Pastoris  

Oleh:

Gerngross, Tillman U. ; Huijuan Li ; Sethuraman, Natarajan ; Stadheim, Terrance A. ; Dongxing Zha ; Prinz, Bianka ; Ballew, Nicole ; Bobrowicz, Piotr ; Byung-Kwon Choi ; Cook, W. James ; Cukan, Michael ; Houston-Cummings, Nga Rewa ; Davidson, Robert ; Bing, Gong ; Hamilton, Stephen R. ; Hoopes, Jack P. ; Youwei, Jiang ; Kim, Nam ; Mansfield, Renee ; Nett, Juergen H. ; Rios, Sandra ; Strawbridge, Rendall ; Wildt, Stefan

Jenis: Article from Journal - ilmiah internasional
Dalam koleksi: Nature Biotechnology: The Science and Business of Biotechnology vol. 24 no. 2 (Feb. 2006), page 210-215.
Topik: antibodies; humanized; glycoengineered

Ketersediaan

Perpustakaan Pusat (Semanggi) Nomor Panggil: NN9.4 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada

Lihat Detail Induk

Isi artikel

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 secrets mAbs with lycosylation 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 demonstrated that human anitbodies with specific human N-Glycan structures can be produced in glyco engineered 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-Gylcosylation.

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