Abstract
We have previously shown that the glucosidase inhibitor, NBDNJ, prevents HBV virion but not subviral particle secretion from stably transfected HepG2 cells (Block et al, 1994). Moreover, the inhibition of virion secretion was due to the inhibition of the ER glucosidase (Lu et al, 1995). To determine which envelope protein functions require glycan processing and to understand the consequences to a glycoprotein of bearing unprocessed glycan, it was of interest to know the specific steps in the virus life cycle which were upset in cells in which ER glucosidase was inhibited
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
Literature Cited
Barinaga, 1993, Secrets of secretion revealed, Science, 260: 488–9
Beasley, R. P. (1988). The Hepatitis B virus. The major etiology of hepatocellular carcinoma. Cancer. 61: 1942–1956..
Block, T., Platt, F., Xuanyong, L., Gerlich, W., Foster, G., Blumberg, B., Dwek, R. Secretion of human hepatitis B virus is inhibited by the imino sugar, N-butyldeoxynojirimycin. Proc. Natl. Acad. Sci. (USA) 91: 2235–2239.
Bruss, V., D. Ganem. (1991). The role of envelope proteins in hepatitis b virus assembly. Proc. Natl. Acad. Sci. USA. 88: 1059–1063.
Chen, W., J. Helenius, I. Braakman and A. Helenius (1995). Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc. Natl. Scad. Sci. (USA). 92: 6229–6233.
Datema, S. Olofsson, P. Romero. (1987), Inhibitors of protein glycosylation and glycoprotein processing in viral systems. Pharmacol. Thera., 33: 221–286
Dwek, R. A. (1995). Glycobiology: more functions for oligosaccharides. Science. 269: 1234–1235.
Elbein, A. D. (1991) Amino sugar compounds as antiviral and anti tumor agents, Sem. cell Biol., 2; 309–317
Fischl, M., L. Resnick, R. Coombs, A. Kremer, J. Potage et al (1994), The safety and efficacy of combination therapy N-butyl deoxynojirimycin (SC-48334) and Zidovudine in patients with HIV infection and 200–500 CD4 cells/ mm3. J. Acq. Imm. Def. S., 7: 139–147
Ganem, D. (1991) Assembly of hepadnavirus virions and subviral particles. In: Hepadnaviruses, Current topics in Microbiol, and Immunol. (W. Mason and C. Seeger, Eds.) 168: 61–84
Gerlich, W. (1993) Structure and molecular biology (of HBV). In: Zuckerman, A. & H. C. Thomas, Viral hepatitis, pp. 83–113. Chruchill Livingston Publishers, London, UK.
Hammand and Helenius, 1994a, Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, Intermediate compartment and Golgi Apparatus, JCB, 126: 41–52).
Hammond, C., and A. Helenius, 1994b, Folding of VSV G protein: sequential interaction with BIP and calnexin. Science. 266: 456458.
Hammond, C., I. Braakman and A. Helenius, 1994, Role of N linked oligosaccharide recognition, glucose trimming and calnexin in glycoprotein folding and quality control. Proc. Natl Acad. Sci.. 91: 913–917
Haas, I. G. and Wabl (1983). Immunoglobulin heavy chain binding protein. Nature. 306: 387–389.
Heerman, H-H, Goldman, I., Schwartz, W., Seyffarth, T., Baumgarten, H. Gerlich, W. H. Large surface proteins of hepatitis b virus containing preS sequence. (1984) J. Virol 52: 396–402)
Heermann, K-H, Gerlich, W.H. (1992), In: Mol. Biol of HBV, A Maclachlan, ed, CRC Press, Boca R raton Fl
Helenius, A. (1994) How N linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell. 5: 253–265.
Herbert, D. N., B. Foellmer and A. Helenius (1995). Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell. 81: 425–433.
Huovila, A. P., A. Eder and S. Fuller (1992) Hepatitis B surface antigen assembles in a post ER, pre golgi compartment. J. Cell Biol. 118: 1305–1320.
Karlsson, G.B., Butters, T. D., Dwek, R.A., Platt, F.M., (1993) Effects of the imino sugar N butyldeoxynojirimycin on the N glycosylation of recombinant gp120 J. Biol. Chem., 268: 570–576.
Kim, P. S. and P. Arvin (1995) Calnexin and BiP as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J. Cell Biol. 128: 29–38.
Leavitt, R., Schlesinger, S., Kornfeld, S. 1979. Impaired intracellular migration and altered solubility of of non glycosylated glycoproteins of vesicular stomatitis virus. J. Biol. Chem. 252: 9018–9023
Lenter, M. and D. Vestweber (1994). The integrin chains b1 and a6 associate with the chaperon calnexin prior to integrin assembly. J. Biol. Chem. 269: 12263–12268.
Lodish, H., A. Kong (1984). Glucose removal from N linked oligosacchairdes is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulim to the Golgi compartment. J. Cell. Biol. 98: 1720–1729.
Lu, X., A. Mehta, T. Butters, R. Dwek and T. Block (1995) Evidence that N-linked glycosylation is necessary for hepatitis B virus secretion. Virol. 213: 660–665.
Lu, X., T. Block and W. Gerlich (1996) Protease induced infectivity of human hepatitis B virus for continuous cultures of human liver cells. J. Virol., in press.
Lu, X., A. Mehta, M. Dadmarz, B. Blumberg, R. Dwek and T. Block (1997) Aberrant trafficking of hepatitis B virus glycoproteins in cells in which N-glycan processing is inhibited. Proc. Natl. Acad. Sci. USA, vol 94: 2380–2385.
Lubas, W.A., Spiro, R.G. (1988). Evaluation of the role of rat liver golgi endo alpha mannosidase in processing N linked oligosaccharides. J. Biol. Chem. 263: 3990–3998.
Mehta, A., X. Lu, T. Block, B. Blumberg, R. Dwek (1996) Similar glycoproteins with drastically different sensities to glycosylation processing (Submitted).
Moore, S. and R. Spiro (1993). Inhibiton of glucopse triming by castaospermine results in rapid degradation od unassembled major histocompatribility complex class I molecules. J. Biol. Chem. 268: 3809–3812.
Moore, S. E. and R. G. Spiro (1990) Demonstration that Golgi Endo-a-mannosidase provides a glucosidase-independent pathway for the formation of complex N-linkied oligosaccharides og glycoproteins. J. Biol. Chem. 265: 1304–13112.
Otteken, A. and B. Moss (1996) Calreticulin interacts with newly synthesized human immunodeficiency virus type I envelope glycoproetin, suggesting a chaperone function similar to that of calnexin. J. Biol. Chem. 271: 97–103.
Ou, W. J., P. H. Cameron, D. Y. Thomas and J. J. M. Bergeron (1993) Association of folding intermediates of glycoproteins with calnexin. Nature. 364: 771–776.
Parent, B., T-K. Yeo and K. Olden (1986). Differential effects of 1-deoxynojirimycin on the intracellular transfport of sceretory glycoprotiens in human hepatoma cells in culture. Mol. Cell. Biochem. 72: 21–33.
Patzer, E., Nakamura, G., Yaffe, A., Intracellular transport and secretion of hepatitis B surface antigen in mammalian cells. (1984), J. Virol., 51: 346–353
Patzer, E.J., Nakamura, G.R., Simonsen, G.C., Levinson, A.L., Brands, R.(1986), Intracellular packaging and assembly of hepatitis b surface antigen particles occurs in the endoplasmic reticulim. J. Virol. 58: 884–892
Pelham, H. R. B. (1991) Recycling of proteins between the endoplasmic reticulum and the Golgi complex. Curr. Opin. Cell Biol. 3: 585–591.
Perrillo, R.P., Schift, ER, Davis, GL, Bodenheimer, HC, Lindsay, K., Payne, J., Dienstag, JL, O’Brien, C., Tamburro, C., Jacobson, IM, Sampliner, R., Feit, D., Lefkowitch, J., Kuhns, M., Meschievitz, C., Sanghvi, B., Albrecht, J., Gibas, A. (1990), A randomized controlled trial of interferon alpha 2b alone and after prednisone withdrawal for the treatment of chronic hepatitis b. New Eng. J. Med. 323: 295–301..
Peterson,, DL, (1981), Isolation and characterization of the major protein and glycoprotein of hepatitis B surface antigen. J. Biol. Chem., 256: 6975–6983
Platt F. G. Nieses, R. Dwek, T. Butters, (1994), NBDNJ is a novel inhibitor of glycolipid biosynthesis, J. Biol. Chem., 269: 8362–8365
Platt, F., G. B. Karlsson & G. S. Jacob, (1992), Modulation of cell surface transferrin receptor by the imino sugar N butyldeoxynojirimycin. Eur. J. Biochem. 208: 187–193.
Rothman, J. E. and L. Orci (1992) Molecular dissection of the secretory pathway. Nature. 355: 409–415.
Saunier, B., Kilker, R.D., Tkacz, J.S., Quaroni, A., Herscovics, A.C. Inhibition of N linked complex oligosaccharide formation by 1 deoxynojirimycin. (1982). J. Biol. Chem. 257: 14155–14161.
Sells, M.A., M. L. Chen, G. Acs, (1987). Production of hepatitis b virus particles in Hep G2 cells transfected with cloned hepatitis b virus DNA. Proc. Natl. Acad. Sci. USA. 84: 1005–1009.
Summers, J., Mason, W.H. (1982). Replication of the genome of hepatitis b virus by reverse transcription of an RNA intermediate. Cell. 29: 403–415.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media New York
About this chapter
Cite this chapter
Block, T.M., Lu, X., Mehta, A., Park, J., Blumberg, B.S., Dwek, R. (1998). Role of Glycan Processing in Hepatitis B Virus Envelope Protein Trafficking. In: Axford, J.S. (eds) Glycoimmunology 2. Advances in Experimental Medicine and Biology, vol 435. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5383-0_20
Download citation
DOI: https://doi.org/10.1007/978-1-4615-5383-0_20
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-7457-2
Online ISBN: 978-1-4615-5383-0
eBook Packages: Springer Book Archive