This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Patzer, E J Articles by Yaffe, A Search for Related Content PubMed PubMed Citation Articles by Patzer, E J Articles by Yaffe, A

 Previous Article  |  Next Article 

J Virol. 1984 August; 51(2): 346-353

Intracellular transport and secretion of hepatitis B surface antigen in mammalian cells.

ABSTRACT

The oligosaccharide processing and secretion of hepatitis B surface antigen (HBsAg) was studied in Chinese hamster ovary cells stably transfected with the gene coding HBsAg. HBsAg was secreted from cells with a relatively long half time (ca. 5 h). This appeared to be a characteristic of HBsAg itself, since HBsAg-producing cells infected with vesicular stomatitis virus transported the viral envelope glycoprotein to the cell surface with normal kinetics (half time of ca. 30 min). The secreted HBsAg was comprised of both the unglycosylated (P20) and the glycosylated (G25) polypeptides, characteristic of HBsAg isolated from human serum or secreted from other cell lines (C. W. Crowley, C.-C. Liu, and A. D. Levinson, Mol. Cell. Biol. 3:44-55, 1983; M. F. Dubois, C. Pourcel, S. Rousset, C. Chang, and P. Tiollais, Proc. Natl. Acad. Sci. U.S.A. 77:4549-4553, 1980; C.-C. Liu, D. Yansura, and A. D. Levinson, DNA, 1:213-221, 1982; G. M. Macnab, J. J. Alexander, G. Lecatsas, E. M. Bey, and J. M. Urbanocvicz, Br. J. Cancer, 24:509-515, 1976; A. M. Moriarity, B. H. Hoyer, J. W.-K. Shih, J. L. Gerin, and D. H. Hamer, Proc. Natl. Acad. Sci. U.S.A. 78:2606-2610, 1981; D. L. Peterson, J. Biol. Chem., 256:6975-6983, 1981). The glycosylated polypeptide (GP25) contained complex oligosaccharide chains. Cell-associated HBsAg also was comprised of both an unglycosylated and a glycosylated polypeptide; however, the glycosylated form (GP23) contained only high-mannose oligosaccharide chains. No oligosaccharide processing of the high-mannose chains could be detected within the cells. Thus, most of the time before secretion of HBsAg from cells must have been spent in a pre-Golgi or early Golgi compartment. Glycosylation was inhibited completely by tunicamycin, although unglycosylated particles were still secreted from cells and were antigenic. The secretion and oligosaccharide processing of HBsAg were inhibited with high concentrations of monensin, but at lower concentrations of monensin HBsAg was still secreted, although only half of the oligosaccharide chains were processed to the complex form.

This article has been cited by other articles:

• Dougherty, A. M., Guo, H., Westby, G., Liu, Y., Simsek, E., Guo, J.-T., Mehta, A., Norton, P., Gu, B., Block, T., Cuconati, A. (2007). A Substituted Tetrahydro-Tetrazolo-Pyrimidine Is a Specific and Novel Inhibitor of Hepatitis B Virus Surface Antigen Secretion. Antimicrob. Agents Chemother. 51: 4427-4437 [Abstract] [Full Text]  
• Blanchet, M., Sureau, C. (2006). Analysis of the Cytosolic Domains of the Hepatitis B Virus Envelope Proteins for Their Function in Viral Particle Assembly and Infectivity. J. Virol. 80: 11935-11945 [Abstract] [Full Text]  
• Rost, M., Mann, S., Lambert, C., Doring, T., Thome, N., Prange, R. (2006). {gamma}2-Adaptin, a Novel Ubiquitin-interacting Adaptor, and Nedd4 Ubiquitin Ligase Control Hepatitis B Virus Maturation. J. Biol. Chem. 281: 29297-29308 [Abstract] [Full Text]  
• Shaw, K. L., Lindemann, D., Mulligan, M. J., Goepfert, P. A. (2003). Foamy Virus Envelope Glycoprotein Is Sufficient for Particle Budding and Release. J. Virol. 77: 2338-2348 [Abstract] [Full Text]  
• Werr, M., Prange, R. (1998). Role for Calnexin and N-Linked Glycosylation in the Assembly and Secretion of Hepatitis B Virus Middle Envelope Protein Particles. J. Virol. 72: 778-782 [Abstract] [Full Text]  
• Mehta, A., Lu, X., Block, T. M., Blumberg, B. S., Dwek, R. A. (1997). Hepatitis B virus (HBV) envelope glycoproteins vary drastically in their sensitivity to glycan processing: Evidence that alteration of a single N-linked glycosylation site can regulate HBV secretion. Proc. Natl. Acad. Sci. USA 94: 1822-1827 [Abstract] [Full Text]  
• Marzolo, M. P., Bull, P., Gonzalez, A. (1997). Apical sorting of hepatitis B surface antigen (HBsAg) is independent of N-glycosylation and glycosylphosphatidylinositol-anchored protein segregation. Proc. Natl. Acad. Sci. USA 94: 1834-1839 [Abstract] [Full Text]