Glycosylation engineering of antibodies for improving...

Details Glycosylation engineering of antibodies for improving... Glycosylation engineering of antibodies for improving...

2011-03-15

2011-03-15

Ketter, James S (Department: 1636)

Chemistry: molecular biology and microbiology

Animal cell, per se ; composition thereof; process of...

Rodent cell, per se

C435S193000

Reexamination Certificate

active

07906329

ABSTRACT:
The present invention relates to the field glycosylation engineering of proteins. More particular, the present invention is directed to the glycosylation engineering of proteins to provide proteins with improved therapeutic properties, e.g., antibodies, antibody fragments, or a fusion protein that includes a region equivalent to the Fc region of an immunoglobulin, with enhanced Fc-mediated cellular cytotoxicity.

REFERENCES:
patent: 4215051 (1980-07-01), Schroeder et al.
patent: 4946778 (1990-08-01), Ladner et al.
patent: 4978745 (1990-12-01), Schoemaker et al.
patent: 5047335 (1991-09-01), Paulson et al.
patent: 5529922 (1996-06-01), Chapman et al.
patent: 5547933 (1996-08-01), Lin
patent: 5736137 (1998-04-01), Anderson et al.
patent: 5753229 (1998-05-01), Mordoh et al.
patent: 5776456 (1998-07-01), Anderson et al.
patent: 5843439 (1998-12-01), Anderson et al.
patent: 5939068 (1999-08-01), Brams et al.
patent: 5952203 (1999-09-01), Withers et al.
patent: 5958403 (1999-09-01), Strom et al.
patent: 6153433 (2000-11-01), Miyoshi et al.
patent: 6183744 (2001-02-01), Goldenberg
patent: 6602684 (2003-08-01), Umaña et al.
patent: 7517670 (2009-04-01), Umaña et al.
patent: 2003/0175884 (2003-09-01), Umaña et al.
patent: 2002307037 (2002-10-01), None
patent: 0 475 354 (1992-03-01), None
patent: 0 669 836 (1996-07-01), None
patent: 0 752 248 (1997-01-01), None
patent: WO 94/11026 (1994-05-01), None
patent: WO 95/24494 (1995-09-01), None
patent: WO 97/30087 (1997-08-01), None
patent: WO 97/30087 (1997-08-01), None
patent: WO 98/06835 (1998-02-01), None
patent: WO 99/54342 (1999-10-01), None
patent: WO 02/079255 (2002-10-01), None
Raju et al., Glycobiology, vol. 10, 2000, pp. 477-486.
Shinkawa et al., The Journal of Bioogical Chemistry, vol. 278, 2003, pp. 3466-3473.
Amstutz, H., et al., “Production and Characterization of a Mouse/Human Chimeric Antibody Directed Against Human Neuroblastoma,”Int. J. Cancer53:147-152, Wiley-Liss, Inc. (1993).
Anderson, W.F., “Human gene therapy,”Nature392:25-30, Nature Pub. Co. (1998).
Arathoon, W.R., and Birch, J.R., “Large-Scale Cell Culture in Biotechnology,”Science232:1390-1395, American Association for the Advancement of Science (1986).
Bailey, J.E., “Toward a Science of Metabolic Engineering,”Science252:1668-1675, American Association for the Advancement of Science (1991).
Bailey, J.E., et al., “Engineering Glycosylation in Animal Cells,” inNew Developments and New Applications in Animal Cell Technology,Merten, O.W., et al., eds., Kluwer Academic Publishers, The Netherlands, pp. 5-23 (1998).
Bailey, J.E., et al., “Metabolic Engineering of N-Linked Glycoform Synthesis Systems in Chinese Hamster Ovary (CHO) Cells,” inAnimal Cell Technology,Carrondo, M.J.T., et al., eds., Kluwer Academic Publishers, The Netherlands, pp. 489-494 (1997).
Bibila, T.A., and Flickinger, M.C., “A Model of Interorganelle Monoclonal Antibody Transport and Secretion in Mouse Hybridoma Cells,”Biotechnol. Bioeng.38:767-780, John Wiley & Sons, Inc. (1991).
Bibila, T.A., and Robinson, D.K., “In Pursuit of the Optimal Fed-Batch Process for Monoclonal Antibody Production,”Biotechnol. Prog.11:1-13, American Chemical Socieety and American Institute of Chemical Engineers (1995).
Bitter, G.A., “Heterologous Gene Expression in Yeast,”Meth. Enzymol.152:673-684, Academic Press, Inc. (1987).
Bitter, G.A., et al., “Expression and Secretion Vectors for Yeast,”Meth. Enzymol.153:516-544, Academic Press, Inc. (1987).
Bretscher, M.S., and Munro, S., “Cholesterol and the Golgi Apparatus,”Science261:1280-1281, American Association for the Advancement of Science (1993).
Briles, E.B., et al., “Isolation of Wheat Germ Agglutinin-resistant Clones of Chinese Hamster Ovary Cells Deficient in Membrane Sialic Acid and Galactose,”J. Biol. Chem.252:1107-1116, American Society for Biochemistry and Molecular Biology, Inc. (1977).
Brisson, N., et al., “Expression of a bacterial gene in plants by using a viral vector,”Nature310:511-514, Nature Pub. Co. (1984).
Brockhausen, I., et al., “Control of glycoprotein synthesis. Characterization of (1→4)-N-acetyl-β-D-glucosaminyltransferases acting on the α- D-(1→3)- and α-D-(1→6)-linked arms ofN-linked oligosaccharides,”Carbohydrate Res.236:281-299, Elsevier Science Publishers B.V. (1992).
Broglie, R., et al., “Light-Regulated Expression of a Pea Ribulose-1,5- Biphosphate Carboxylase Small Subunit Gene in Transformed Plant Cells,”Science224:838-843, American Association for the Advancement of Science (1984).
Campbell, C., and Stanley, P., “A Dominant Mutation to Ricin Resistance in Chinese Hamster Ovary Cells Induces UDP-GlcNAc:Glycopeptide β-4-N-Acetylglucosaminyltransferase III Activity,”J. Biol. Chem.261:13370-13378, American Society for Biochemistry and Molecular Biology, Inc. (1984).
Caruthers, M.H., et al., “New chemical methods for synthesizing polynucleotides,”Nuc. Acids Res. Symp. Series7:215-223, IRL Press Limited (1980).
Chow, F., et al., “Synthesis of oligodeoxyribonucleotides on silica del support,”Nuc. Acids Res.9:2807-2817, IRL Press Limited (1981).
Cole, N.B., et al., “Diffusional Mobility of Golgi Proteins in Membranes of Living Cells,”Science273:797-801, American Association for the Advancement of Science (1996).
Cole, S.P.C., et al., “The EBV-Hybridoma Technique and its Application to Human Lung Cancer,” inMonoclonal Antibodies and Cancer Therapy,Reisfeld, R.A., and Sell, S., eds., Alan R. Liss, Inc., New York, NY, pp. 77-96 (1985).
Coruzzi, G., et al., “Tissue-specific and light-regulated expression of a pea nuclear gene encoding the small subunit of ribulose-1,5-biphosphate carboxylase,”EMBO J.3:1671-1679, IRL Press Limited (1984).
Cote, R.J., et al., “Generation of human monoclonal antibodies reactive with cellular antigens,”Proc. Natl. Acad. Sci.80:2026-2030, The National Academy of Sciences (1983).
Crea, R., and Horn, T., “Synthesis of oligonucleotides on cellulose by a phosphotriester method,”Nuc. Acids Res.8:2331-2348, IRL Press Limited (1980).
Creighton, T.E.,Proteins: Structures and Molecular Principles,W.H. Freeman and Co., New York, NY, pp. 34-60 (1983).
Cumming, D.A., “Glycosylation of recombinant protein therapeutics: control and functional implications,”Glycobiology1:115-130, Oxford University Press (1991).
Dörr, U., et al., “First Clinical Results with the Chimeric Antibody chCE7 in Neuroblastoma. Targeting Features and Biodistribution Data,”Eur. J. Nucl. Med.20:858, Springer International (1993).
Dennis, J.W., et al., “β1-6 Branching of Asn-Linked Oligosaccharides Is Directly Associated with Metastasis,”Science236:582-585, American Association for the Advancement of Science (1987).
Do, K-Y., “Modification of Glycoproteins byN-Acetylglucosaminyltransferase V Is Greatly Influenced by Accessibility of the Enzyme to Oligosaccharide Acceptors,”J. Biol. Chem.269:23456-23464, American Society for Biochemistry and Molecular Biology (1994).
Dunphy, W.G., and Rothman, J.E., “Compartmentation of Asparagine-linked Oligosaccharide Processing in the Golgi Apparatus,”J. Cell. Bio.97:270-275, Rockefeller University Press (1983).
Dunphy, W.G., et al., “Attachment of Terminal N-Acetylglucosamine to Asparagine-Linked Oligosaccharide Occurs in Central Cisternae of the Golgi Stack,”Cell40:463-472, MIT (1985).
Dunphy, W.G., et al., “Early and late functions associated with the Golgi apparatus reside in distinct compartments,”Proc. Natl. Acad. Sci.78:7453-7457, The National Academy of Sciences (1981).
Dwek, R.A., “Glycobiology: More Functins for Oligosaccharides,”Science269:1234-1235, American Association for the Advancement of Science (1995).
Easton, E.W., e

Affiliated with

Also associated with

Rating

Glycosylation engineering of antibodies for improving... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Glycosylation engineering of antibodies for improving..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Glycosylation engineering of antibodies for improving... will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-2744926