Chaperones involved in hepatitis B virus morphogenesis

Biological Chemistry

Volumn 380, Issue 3, 1999, Pages 305-314

  Prange, Reinhild ^a   Werr, Margaret ^a   Löffler Mary, Heike ^a  

^a JOHANNES GUTENBERG UNIVERSITY   (Germany)

Author keywords

Calnexin; Hsc70; Membrane proteins; Posttranslational; Protein translocation

Indexed keywords

CALNEXIN; CHAPERONE; GLYCAN; GLYCINE CLEAVAGE SYSTEM; HEAT SHOCK PROTEIN 70; M PROTEIN; MEMBRANE PROTEIN; NUCLEOCAPSID PROTEIN; VIRUS ENVELOPE PROTEIN;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; GENE STRUCTURE; HEPATITIS B VIRUS; HOST CELL; LIVER CELL; MEMBRANE STRUCTURE; MORPHOGENESIS; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT; RECEPTOR BINDING; VIROGENESIS; VIRUS ASSEMBLY; VIRUS NUCLEOCAPSID;

ANIMALIA; HEPATITIS B VIRUS; MIRIDAE;

EID: 0033005078     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.1999.042     Document Type: Article

References (36)

1. Bergeron, J.J.M., Brenner, M.B., Thomas, D.Y., and Williams, D.B. (1994). Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. Trends Biochem. Sci. 19, 124-128.
2. Block, T.M., Lu, X., Platt, F.M., Foster, G.R., Gerlich, W.H., Blumberg, B.S., and Dwek, R.A. (1994). Secretion of human hepatitis B virus is inhibited by the imino sugar N-butyldeoxynojirimycin. Proc. Natl. Acad. Sci. USA 91, 2235-2239.
3. Brodsky, J.L. (1996). Post-translational protein translocation: not all Hsc70s are created equal. Trends Biochem. Sci. 21, 122-126.
4. Bruss, V. (1997). A short linear sequence in the pre-S domain of the large hepatitis B virus envelope protein required for virion formation. J. Virol. 77, 9350-9357.
5. Bruss, V., and Ganem, D. (1991). The role of envelope proteins in hepatitis B virus assembly. Proc. Natl. Acad. Sci. USA 88, 1059-1063.
6. Bruss, V., and Vieluf, K. (1995). Functions of the internal pre-S domain of the large surface protein in hepatitis B virus particle morphogenesis. J. Virol. 69, 6652-6657.
7. Bruss, V., Lu, X., Thomssen, R., and Gerlich, W.H. (1994). Post-translational alterations in transmembrane topology of the hepatitis B virus large envelope protein. EMBO J. 13, 2273-2279.
8. Bukau, B., and Horwich, A.L. (1998). The hsp70 and hsp60 chaperone machines. Cell 92, 351-366.
9. Cannon, K.S., Hebert, D.N., and Helenius, A. (1996). Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin. J. Biol. Chem. 271, 14280-14284.
10. Eble, B.E., MacRae, D.R., Lingappa, V., and Ganem, D. (1987). Multiple topogenic sequences determine the transmembrane orientation of hepatitis B surface antigen. Mol. Cell. Biol. 7, 3591-3601.
11. Eble, B.E., Lingappa, V.R., and Ganem, D. (1990). The N-terminal (pre-S2) domain of a hepatitis B virus surface glycoprotein is translocated across membranes by downstream signal sequences. J. Virol. 64, 1414-1419.
12. Fernholz, D., Galle, P.R., Stemler, M., Brunetto, M., Bonino, F., and Will, H. (1993). Infectious hepatitis B virus variant defective in pre-S2 protein expression in a chronic carrier. Virology 794, 137-148.
13. Gallina, A., Gazina, E., and Milanesi, G. (1995). A C-terminal preS1 sequence is sufficient to retain hepatitis B virus L protein in 293 Cells. Virology 213, 57-69.
14. Guo, J.-T., and Pugh, J.C. (1997). Topology of the large envelope protein of duck hepatitis B virus suggests a mechanism for membrane translocation during particle morphogenesis. J. Virol. 71, 1107-1114.
15. Hebert, D.N., Foellmer, B., and Helenius, A. (1995). Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81, 425-433.
16. Heermann, K.H., and Gerlich, W.H. (1991). Surface proteins of hepatitis B viruses. In: Molecular Biology of the Hepatitis B Virus, A. McLachlan, ed. (Boca Raton, FL, USA: CRC Press, Inc.), pp. 109-143.
17. Hendrick, J.P., and Hartl, F.-U. (1993). Molecular chaperonefunctions of heat-shock proteins. Ann. Rev. Biochem. 62, 349-384.
18. Hildt, E., Saher, G., Bruss, V., Hofschneider, P.H. (1996). The hepatitis B virus large surface protein (LHBs) is a transcriptional transactivator. Virology 225, 235-239.
19. Huovila, A.J., Eder, A.M., and Fuller, S.D. (1992). Hepatitis B surface antigen assembles in a post-ER, pre-Golgi compartment. J. Cell Biol. 118, 1305-1320.
20. Löffler-Mary, H., Werr, M., and Prange, R. (1997). Sequence-specific repression of cotranslational translocation of the hepatitis B virus envelope proteins coincides with binding of heat shock protein Hsc70. Virology 235, 144-152.
21. Lu, X., Metha, A., Dwek, R., Butters, T., and Block, T. (1995). Evidence that N-linked glycosylation is necessary for hepatitis B virus secretion. Virology 213, 660-665.
22. Metha, A., Lu, X., Block, T.M., Blumberg, B.S., and 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.
23. Nassal, M. (1996). Hepatitis B virus morphogenesis. CTMI, 297-337.
24. Neurath, A.R., Kent, S.B.H., Strick, N., and Parker, K. (1986). Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus. Cell 46, 429-436.
25. Ostapchuk, P., Hearing, P., and Ganem, D. (1994). A dramatic shift in the transmembrane topology of a viral envelope glycoprotein accompanies hepatitis B viral morphogenesis. EMBO J. 13, 1048-1058.
26. Ou, W.J., Cameron, P.H., Thomas, D.Y., and Bergeron, J.J.M. (1993). Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364, 771-776.
27. Prange, R., and Streeck, R.E. (1995). Novel transmembrane topology of the hepatitis B virus envelope proteins. EMBO J. 14, 247-256.
28. Rapoport, T.A., Jungnickel, B., and Kutay, U. (1996). Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65, 271-303.
29. Stirk, H.J., Thornton, J.M., and Howard, C.R. (1992). A topological model for hepatitis B surface antigen. Intervirology 33, 148-158.
30. Summers, J., Smith, P.M., and Horwich, A.L. (1990). Hepadnavirus envelope proteins regulate covalently closed circular DNAamplification. J. Virol. 64, 2819-2824.
31. Swameye, I., and Schaller, H. (1997). Dual topology of the large envelope protein of duck hepatitis B virus: determinants preventing pre-S translocation and glycosylation. J. Virol. 71, 9434-9441.
32. Ueda, K., Tsurimoto, T., and Matsubara, K. (1991). Three envelope proteins of hepatitis B virus: large S, middle S, and major S proteins needed for the formation of Dane particles. J. Virol. 65, 3521-3529.
33. Werr, M., and 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.
34. Williams, D.B. (1995). Calnexin: a molecular chaperone with a taste for carbohydrate. Biochem. Cell Biol. 73, 123-132.
35. Xu, Z., Bruss, V., and Yen, T.S.B. (1997). Formation of intracellular particles by hepatitis B virus large surface protein. J. Virol. 71, 5487-5494.
36. Zimmermann, R. (1998). The role of molecular chaperones in protein transport into the mammalian endoplasmic reticulum. Biol. Chem. 379, 275-282.