Chapter 103
Metabolic Engineering Glycosylation: Biotechnology's Challenge to the Glycobiologist in the Next Millennium
Prof. Dr. Beat Ernst,
Prof. Dr. Gerald W. Hart,
Prof. Dr. Pierre Sinaý,
Prof. Dr. Beat Ernst
Institut für Molekulare Pharmazie, Universität Basel, Klingenbergstrasse 50, 4051 Basel, Switzerland
Search for more papers by this authorProf. Dr. Gerald W. Hart
Dept. of Biological Chemistry, Johns Hopkins University School of Medicine, 725 N. Wolf St. Rm., 401 Hunterian Baltimore, MD 21205-2185, USA
Search for more papers by this authorProf. Dr. Pierre Sinaý
Dept. de Chimie, URA 1686, Ecole Normale Supérieure, 24 rue Lhomond, 75231 Paris Cedex 05, France
Search for more papers by this authorBook Author(s):Prof. Dr. Beat Ernst,
Prof. Dr. Gerald W. Hart,
Prof. Dr. Pierre Sinaý,
Prof. Dr. Beat Ernst
Institut für Molekulare Pharmazie, Universität Basel, Klingenbergstrasse 50, 4051 Basel, Switzerland
Search for more papers by this authorProf. Dr. Gerald W. Hart
Dept. of Biological Chemistry, Johns Hopkins University School of Medicine, 725 N. Wolf St. Rm., 401 Hunterian Baltimore, MD 21205-2185, USA
Search for more papers by this authorProf. Dr. Pierre Sinaý
Dept. de Chimie, URA 1686, Ecole Normale Supérieure, 24 rue Lhomond, 75231 Paris Cedex 05, France
Search for more papers by this authorSummary
The prelims comprise:
-
Introduction
-
Recent Developments in Carbohydrate Biosynthesis
-
Glycosylation Engineering Alternate Expression Hosts For Recombinant Protein Therapeutic Production
-
Summary
References
- Cumming, D. A., Glycosylation of recombinant protein therapeutics: control and functional implications. Glycobiology, 1991, 1, 115–130.
- Jenkins, N. and Curling, E.M.A., Glycosylation of recombinant proteins: problems and prospects. Enzyme Microb. Technol., 1994, 16, 354–364.
- Jenkins, N., Parekh, R. B., James, D. C., Getting the glycosylation right: Implications for the biotechnology industry. Nature Biotech., 1996, 14, 975–961.
- Goochee, C. F. and Monica, T., Environmental effects on protein glycosylation. Biotechnology, 1990, 8, 421–427.
- Bailey, J. E., Toward a science of metabolic engineering. Science, 1991, 252, 1668–1675.
- Jacobsen, J. R. and Khosla, C., New directions in metabolic engineering. Curr. Opin. Chem. Biol., 1998, 2, 133–137.
- Stephanopoulos, G., Metabolic engineering. Curr. Biol., 1994, 5, 196–200.
- Cameron, D. C. and Tong, U., Cellular and metabolic engineering. Appl. Biochem. Biotechnol., 1993, 38, 105–140.
- Kundig, W., Ghosh, S., Roseman, S., The sialic acids: N-acyl-D-mannosamine kinase from rat liver. J. Biol. Chem., 1966, 241, 5619–5626.
- Watson, D. R., Jordian, G. W., and Roseman, S., The sialic acids: Sialic acid 9-phosphate synthetase. J. Biol. Chem., 1966, 241, 5627–5636.
- Kean, E. L. and Roseman, S., The sialic acids: Purification and properties of cytidine 5′-monophosphosialic acid synthetase. J. Biol. Chem., 1966, 241, 5643–5650.
- Warren, L. and Felsenfeld, H., The biosynthesis of sialic acids. J. Biol. Chem., 1962, 237, 1421–1431.
- Kornfeld, S., Kornfeld, R., Neufeld, E. F., O'Brien, P. J., The feedback control of sugar nucleotide biosynthesis in liver. Proc. Natl Acad. Sci. USA, 1964, 52, 371–379.
- Hagemeier, C., Vischer, P., and Buddecke, E., Studies on the biosynthesis of N-acetylneuraminic acid in cultured arterial wall cells. Biochem. Soc. Trans., 1986, 14, 1173–1174.
- Thomas, G. H., Reynolds, L. W., Miller, C. S., Overproduction of N-acetylneuraminic acid by sialuria fibroblasts. Pediatr. Res., 1985, 19, 451–455.
-
Gu, X.,
Wang, D. I. C.,
Improvement of interferon-γ sialylation in Chinese hamster ovary cell culture by feeding of N-acetylmannosamine.
Biotech. and Bioeng.,
1998,
58,
642–647.
10.1002/(SICI)1097-0290(19980620)58:6<642::AID-BIT10>3.0.CO;2-9 CAS PubMed Web of Science® Google Scholar
- Eckhardt Muhlenhoff, M., Bethe, A., Gerardy-Schahn, R., Expression cloning of the Golgi CMP-sialic acid transporter. Proc. Natl Acad. Sci, USA, 1996, 93, 7572–7576.
- Ishida, N., Ito, M., Yoshioki, S., Sun-Wada, G. H., Kawakita, M., Functional expression of human Golgi CMP-sialic acid transporter in the Golgi complex of a transporter-deficient Chinese hamster ovary cell mutant. J. Biochem. (Tokyo), 1998, 124, 171–178.
- Eckhardt, M., Gerardy-Schahn, R., Molecular cloning of the hamster CMP-sialic acid transporter. Eur. J. Biochem., 1997, 248, 1878–192.
- Minch, S. L., Kallio, P. T., Bailey, J. E., Tissue plasminogen activator coexpressed in Chinese hamster ovary cells with alpha (2,6)-sialyltransferase contains NeuAc alpha (2,6)Gal beta (1,4) Glc-N-AcR linkages. Biotechnol. Prog., 1995, 11, 348–351.
- Grabenhorst, E., Hoffman, A., Nimtz, A. M., Zettlmeissl, G., Conradt H. S., Construction of stable BHK-21 cell co-expressing human secretory glycoprotein and human Gal(β1–4)GlcNAc-α2,6 sialyltransferase.α2,6 NeuAc is preferentially attached to the Gal((β-1–4)GlcNAc(β-1,2)-Man(α-1,3)-branch of diantennary oligosaccharides from secreted recombinant β-trace. Eur. J. Biochem., 1995, 232, 718–725.
- Jenkins, N., Buckberry L., Marc, A., Monaco, L., Genetic engineering of alpha 2,6-sialyltransferase in recombinant CHO cells. Biochem. Soc. Trans., 1998, 26, S115.
- Zhang, X., Lok, S. H. and Kon, O. L., Stable expression of human alpha-2,6-sialytransferase in Chinese hamster ovary cells; funtional consequences for human erythropoietin expression and bioactivity. Biochiem. Biophys. Acta, 1998, 1425, 441–452.
- Van Rinsum, J., Van Dijk, W., Hooghwinkel, G. J. M., Ferwerda, W., Subcellular localization and tissue distribution of sialic acid precursor forming enzymes. Biochem. J. 1983, 210, 21–28.
- Stasche, R., Hinderlich, S., Weise, C., Effertz, K., Lucka, L., Poormann, P., Reutter, W., A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. J. Biol. Chem., 1997, 272, 24319–24324.
- Hinderlich, S., Stasche, R., Zeitler, R., Reutter, W., A bifunctional enzyme catalyzes the first two steps in N-acetyneuraminic acid biosynthesis of rat liver. J. Biol. Chem., 1997, 272, 24313–24318.
- Maru, I., Ohta, Y., Murata, K., Tsukada, Y., Molecular cloning and identification of N-acyl-D-glucosamine-2-epimerase from porcine kidney as a renin binding protein. J. Biol. Chem. 1996, 271, 16294–16299.
- Schauer, R. and Wember, M., Isolation and characterization of sialate lyase from pig kidney. Biol. Chem. Hoppe Seyler, 1996, 377, 293–239.
- Santell, L., Ryll, T., Etcheverry, T., Santoris, M., Dutina, G., Wang, A., Gunson, J., Warner, T. G., Aberrant metabolic sialylation of recombinant proteins expressed in Chinese hamster ovary cells in large-scale batch cultures, Biochem. Biophys. Res. Comm. 1999, 258, 132–137.
- Diaz, S. and Varki, A., Metabolic labeling of sialic acids in tissue culture cell lines: Methods identify substituted and modified radioactive neuraminic acids. Anal. Biochem., 1985, 150, 32–46.
- Warner, T. G., Chang, J., Ferrari, J., Harris, R., McNerney, T., Bennett, G., Burnier, J., Sliwkowski, M.B., Isolation and properties of a soluble sialidase from the culture fluid of Chinese hamster ovary cells. Glycobiology, 1993, 3, 455–463.
- Chotigeat, W., Watananpokasin, Y., Mahler, S., Gray, P.P., Role of environmental-conditions on the expression levels, glycoform pattern and levels of sialyltransferase for hFSH expression produced by recombinant CHO cells. Cytotechnology, 1994, 15, 217–221.
- Gebert, C. A. and Gray, P.P., Expression of FSH in ChO cells.2. stimulation of hFSH expression levels by defined medium supplements. Cytotechnology, 1994, 14, 39–45.
- Stambolina, D., Ai, Y., Sidjanin, D., Nesburn, K., Stahe, G., Rosenberg, M., Bergsma, D.J., Cloning of the galactokinase cDNA and identification of mutations in two families with cataracts. Nat. Genet., 1995, 10, 307–12.
- Flach, J. E., Reichardt, J. K., Elsas, E. J., Sequence of a cDNA encoding human galactose-1-phosphate uridyl transferase. Mol. Biol. Med., 1990, 7, 365–369.
- Daude, N., Gallaher, T. K., Zeschnigk, M., Starzinski-Powitz, A., Petry, K. G., Haworth, I. S., Reichardt, J. K., Molecular cloning, characterization, and mapping of a full-length cDNA encoding human UDP-galactose 4′epimerase. Biochem. Mol. Med., 1995, 56, 1–7.
- Segal, S., Galactosaemia today: the enigma and the challenge. J. Inherit. Metab. Dis., 1998, 21, 455–471.
- Wang, B. B., Xu, Y. K., Ng, W. G., Wong, L. J., Molecular and biochemical basis of galactosemia. Mol. Genet. Metab., 1998, 63, 263–269.
- Mulkerrin, M.G., Raju, S., Gazzano-santoro, H., Gray, R., Parker, M., Bjork, N., Raffo, W., Borge, S., Chen, A. B., Ultsch, M., DeVos, A. M., Antibody mediated cell killing depends on the structure of the Fc oligosaccharide. Second symposium on analysis of well characterized biotechnology Pharmaceuticals, San Francisco, 1998.
- Boyd, P.N., Line, A.C., Patel, A.K., The effect of the removal of sialic acid, galactose and totae carbohydrate on the functional activity of campath. In. Mol. Immunol. 1995, 32, 1311–1318.
- Gawlitzek, M., Santell, L., Papac, D., Warner, T. G., unpublished observations.
- Garnick, R. L., Raw materials as a source of contamination in large-scale cell culture. Dev. Biol. Stand., 1998, 93, 21–29.
- Lu, M. and Kleckner, M., Molecular cloning and characterization of the pgm gene encoding phosphoglucomutase of Escherichia coli. J. Bacteriol., 1994, 176, 5847–5851.
- Hossain, S. A., Tanizawa, K., Kazuta, Y., Fukui, T., Overproduction and characterization of recombinant UDP-glucose pyrophosphorylase from Escherichia coli K-12. J. Biochem. (Tokyo), 1994, 115, 965–972.
- Narimatsu, H., Sinha, S., Brew, K., Okayama, H., Qasba, P.K., Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1–4) galactosyltransferase. Proc. Natl Acad. Sci. USA, 1986, 83, 4720–4724.
- Panneerselvam, K and Freeze, H.H., Mannose enters mammalian cells using a specific transporter that is insensitive to glucose. J. Biol. Chem., 1996, 271, 9417–9421.
- Alton, G., Hasilik, M., Niehues, R., Panneerselvam, K., Etchison, J. R., Fana, F., Freeze, H. H., Direct utilization of mannose for mammalian glycoprotein biosynthesis. Glycobiology, 1998, 8, 285–295.
- Stibler, H., Holzbach, U., Kristiansson, B., Isoforms and levels of transferrin, antithrombin, alpha (1)-antitrypsin and thyroxine-binding. Scand. J. Clin. Lab. Invest., 1998, 58, 55–61.
- O'Reilly, D. R., Miller, L. K., Luckow, V. A., Baculovirus Expression Vectors, Freeman Press, New York 1992.
- Miller, L. K., Baculoviruses as gene expression vectors. Annu. Rev. Microbiol., 1988, 42, 177–199.
- Jarvis, D. L., Kawar, Z. S., Hollister, J. R., Engineering N-glycosylation pathways in the baculovirus-insect cell system. Curr. Opin. Biotech., 1998, 9, 528–533.
- Altmann, F., More than silk and honey-or, can insect cells serve in the production of therapeutic glycoproteins? Glycoconj. J., 1997, 14, 643–646.
- Jarvis, D. L. and Finn, E. E., Modifying the insect cell N-glycosylation pathway with immediate early baculovirus expression vectors. Nat. Biotech., 1996, 14, 1288–1292.
- Jarvis, D. L. and Finn, E. E., Biochemical analysis of the N-glycosylation pathway in baculovirus-infected lepidopteran insect cells. Virology, 1995, 212, 500–511.
-
Altmann, F.,
N-glycosylation in insects revisited.
Trends Glycosci. Glycotech.,
1996,
40,
101–114.
10.4052/tigg.8.101 Google Scholar
- Altmann, G. Kornfeld, Dalik, T., Staudacher, E., Glossl, J., Processing of asparagine-linked oligosaccharides in insect cells. N-acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells. Glycobiology, 1993, 3, 619–625.
- Velardo, M.A., Bretthauer, R. K., Boutaud, A., Reinhold, B., Rienhold, V.N., Castellino, F. J., The presence of UDP-N-acetylglucosaminyltransferase I activity in Spodoptera frugiperda cells (IPLB-SF-21AE) and its enhancement as a result of bculovirus infection. J. Biol. Chem., 1993, 268, 17902–17907.
- Wagner, R., Liedtke, S., Kretzschmar, E., Geyer, H., Geyer, R., Klenk, H. D., Elongation of the N-glycans of fowl plauge virus hemagglutinin expressed in Spodoptera frugiperda (Sf9) cells by coexpression of human beta 1,2-N-acetylglucosaminyltransferase I. Glycobiology, 1996, 6, 165–175.
- Hollister, J. R., Shaper, H., Jarvis, D. L., Stable expression of mammalian beta 1,4-galactosyltransferase extends the N-glycosylation pathway in insect cells. Glycobiology, 1998, 8, 472–480.
- Traving, C., Roggentin, P., Schauer, R., Cloning, sequencing and expression of the acylneuraminate lyase gene from Clostridium perfringens A99. Glycoconj. J., 1997, 14, 821–830.
- Maru, I., Ohnishi, J., Ohta, Y., Tsukada, Y., Simple and large-scale production of N-acetylneuraminic acid from N-acetyl-D-glucsamine and pyruvate using N-aceyl-D-glucosamine 2-epimerase and N-acetylneuraminate lyase. Carbohydr. Res., 1998, 306, 575–578.
- Munster, A. K., Echkhardt, M., Potvin, B., Muhlenhoff, M., Stanley, P., Gerardy-Schahn, R., Mammalian cytidine 5′-monophosphate N-acetylenuraminic acid synthetase: a nuclear protein with evolutionarily conserved structural motifs. Proc. Natl Acad. Sci. USA, 1998, 95, 9140–9145.
- Tretter, V., Altmann, F., Kubelka, V., Marz, L., Becker, W.M., Fucose alpha 1,3-linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honeybee venom allergic individuals. Int. Arch. Allergy Immunol., 1993, 102, 259–266.
- Van Die, I., Van Tetering, A., Bakker, H., Van den Eijnden, D. H., Joziasse, D. H., Glycosylation in lepidopteran insect cells: identification of a beta 1–4-acetylgalactosaminyltransferase involved in the synthesis of complex-type oligosaccharide chains. Glycobiology, 1996, 6, 157–164.
- Altmann, F., Schwihla, H., Staudaucher, E., Glossl, J., Marz, L., Insect cells contain an unusual, membrane-bound beta-N-acetyglucosaminidase probably involved in the processing of protein N-glycans. J. Biol. Chem, 1995, 270, 17344–17349.
- Fraley, R. T., Rogers, S. G., Horsch, R. B., Sanders, P. B., Flick, J. S., Adams, S. P., Brand, M.L., Fink, C. L., Fry, J. S., Galluppi, G. R., Goldberg, S. P., Hoffmann, N. L., Woo, S. C., Expression of bacterial genes in plant cells. Proc. Natl Acad. Sci. USA, 1983, 80, 1090–1093.
- Larrick, J. W., Yu, L., Chen, J., Jaiswal, S., Production of antibodies in transgenic plants. Res. Immunol., 1998, 149, 603–608.
- Conrad, U. and Fiedler, U., Expression of engineered antibodies in plant cells. Plant Mol. Biol., 1994, 26, 1023–1030.
- Ma, J. K. and Hein, M. B., Plant antibodies for immunotherapy. Plant Physiol. 1995, 109, 341–346.
- Evangelista, R. L., Kusnadi, A. R., Howard, J. A., Nikolov, Z. L., Process and economic evaluation of the extraction and purification of recombinant beta-glucoronidase from transgenic corn. Biotechnol. Prog. 1998, 14, 607–614.
- Lerouge, R., Cabanes-Machetearu, M., Rayon, C., Fischetter-Laine, A., Gomord, V., Faye, L., N-glycoprotein biosynthesis in plants: recent developments and future trends. Plant Mol. Biol., 1998, 38, 31–48.
- Cabanes-Macheteau, M., Fitchette-Laine, A., Loutelier-Bourhis, C., Lange, C., Vine, N. D., Ma, J. K. C., Lerouge, P., and Faye, L., N-glycosylation of a mouse IgG expressed in trans-genic tobacco plants. Glycobiology, 1999, 9, 365–372.
- Hamako, J., Matsui, T., Ozeki, Y., Mizuochi, T., Titani, K., Comparative studies of asparagine-linked sugar chains of immunoglobulin G from eleven mammalian species. Comp. Biochem. Physiol., 1993, 106B, 949–954.
- Raju, T. S., Briggs, J., Borge, S., Wilks, M., Lerner, L., Species specific glycosylation of IgG. Glycobiology, 1998, 8, A104.
- Ashwell, G. and Morell, A.G., The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins. Adv. Enzymology, 1974, 41, 99–128.
- Von Schaewen, A., Sturm, A., O'Neill, J., Chrispeels, M. J., Isolation of a mutant Arabidopsis plant that lacks N-acetyl glucosaminyl transferase I and is unable to synthesize Golgi-modified complex N-linked glycans. Plant Physiol., 1993, 102, 1109–1118.
- Faye, L., Gomord, V., Fitchetter-Laine, A. C., Chrispeels, M. J., Affinity purification of antibodies specific for Asn-linked glycans containing alpha 1,3 fucose or beta 1,2 xylose. Anal. Biochem., 1993, 209, 104–108.
- Garcia-Casado, G., Sanchez-Monge, R., Chrispeels, M. J., Armentia, A., Salcedo, G., Gomez, L., Role of complex asapargine-linked glycans in the allergenicity of plant glycoproteins. Glycobiology, 1996, 6, 471–477.
- Accili, D. and Taylor, S. I., Targeted inactivation of the insulin receptor gene in mouse 3T3-L1 fibroblasts via homologous recombination. Proc. Natl Acad. Sci USA, 1991, 88, 4708–4712.
- Brown, J. P., Wei, W., Sedivy, J. M., Bypass of senescence after disruption of p21CIP1/WAF1 gene in normal diploid human fibroblasts. Science, 1997, 277, 831–834.
- Zheng, H. and Wilson, J. H., Gene targeting in normal and amplified cell lines. Nature, 1990, 344, 170–173.
-
Halfter, U.,
Morris, P. C.,
Willmitzer, L.,
Gene targeting in Arabidopsis thaliana.
Mol. Gen. Genet.,
1992,
23,
186–193.
10.1007/BF00279790 Google Scholar
- Thykjaer, T., Finnemann, J., Schauser, L., Christensen, L., Poulsen, C., Stougaard, J., Gene targeting approaches using positive-negative selection and large flanking regions. Plant Mol. Biol., 1997, 35, 523–530.
- Schuch, W., Using antisense RNA to study gene function. Symp. Soc. Exp. Biol., 1991, 45, 117–127.
- Hamilton, A. J., Fray, R. G., Grierson, D., Sense and antisense inactivation of fruit ripening genes in tomato. Curr. Top. Microbial Immunol, 1995, 197, 77–89.
