Glycan optimization of a human monoclonal antibody in the aquatic plant Lemna minor-Reference-Cited by-同舟云学术

Glycan optimization of a human monoclonal antibody in the aquatic plant Lemna minor

Published:2006-11-26 Issue:12 Volume:24 Page:1591-1597
ISSN:1087-0156
Container-title:Nature Biotechnology
language:en
Short-container-title:Nat Biotechnol

Author:

Cox Kevin M,Sterling Jason D,Regan Jeffrey T,Gasdaska John R,Frantz Karen K,Peele Charles G,Black Amelia,Passmore David,Moldovan-Loomis Cristina,Srinivasan Mohan,Cuison Severino,Cardarelli Pina M,Dickey Lynn F

Publisher

Springer Science and Business Media LLC

Subject

Biomedical Engineering,Molecular Medicine,Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Link

http://www.nature.com/articles/nbt1260.pdf

Reference30 articles.

1. Gasdaska, J., Spencer, D. & Dickey, L. Advantages of therapeutic protein production in the aquatic plant Lemna. Bioprocessing J. 3, 50–56 (2003).

2. Krapp, S., Mimura, Y., Jefferis, R., Huber, R. & Sondermann, P. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J. Mol. Biol. 325, 979–989 (2003).

3. Shinkawa, T. et al. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J. Biol. Chem. 278, 3466–3473 (2003).

4. Shields, R.L. et al. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity. J. Biol. Chem. 277, 26733–26740 (2002).

5. Wright, A. & Morrison, S. Effect of glycosylation on antibody function: Implications for genetic engineering. Trends Biotechnol. 15, 26–32 (1997).

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