Native Hepatitis B Virions and Capsids Visualized by Electron Cryomicroscopy

Molecular Cell

Volumn 22, Issue 6, 2006, Pages 843-850

  Dryden, Kelly A ^a   Wieland, Stefan F ^a   Whitten Bauer, Christina ^a   Gerin, John L ^b   Chisari, Francis V ^a   Yeager, Mark ^a,c  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b GEORGETOWN UNIVERSITY MEDICAL CENTER   (United States)

^c SCRIPPS CLINIC   (United States)

Author keywords

HUMDISEASE

Indexed keywords

GLYCOPROTEIN; LIPID; MEMBRANE PROTEIN; VIRUS DNA;

ANIMAL TISSUE; ARTICLE; CELL ISOLATION; CELL MATURATION; CONTROLLED STUDY; CRYOELECTRON MICROSCOPY; GENE ISOLATION; HEPATITIS B VIRUS; IMAGE ANALYSIS; IMAGE RECONSTRUCTION; LIVER; MOUSE; NONHUMAN; SERUM; STRUCTURE ANALYSIS; TRANSGENIC MOUSE; VIRION; VIRUS CAPSID; VIRUS ENVELOPE; VIRUS MORPHOLOGY; VIRUS PARTICLE;

ANIMALS; CAPSID; CRYOELECTRON MICROSCOPY; DNA, VIRAL; DNA-DIRECTED RNA POLYMERASES; HEPATITIS B; HEPATITIS B VIRUS; HUMANS; IMAGING, THREE-DIMENSIONAL; LIPIDS; LIVER; MICE; MICE, TRANSGENIC; MODELS, MOLECULAR; VIRAL PROTEINS; VIRUS ASSEMBLY;

HEPATITIS B VIRUS; MIRIDAE; MUS MUSCULUS;

EID: 33745207098     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.04.025     Document Type: Article

References (35)

1. Baker T.S., and Cheng R.H. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116 (1996) 120-130
2. Birnbaum F., and Nassal M. Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein. J. Virol. 64 (1990) 3319-3330
3. Böttcher B., Wynne S.A., and Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 386 (1997) 88-91
4. Böttcher B., Tsuji N., Takahashi H., Dyson M.R., Zhao S., Crowther R.A., and Murray K. Peptides that block hepatitis B virus assembly: Analysis by cryomicroscopy, mutagenesis and transfection. EMBO J. 17 (1998) 6839-6845
5. Bruss V. A short linear sequence in the pre-S domain of the large hepatitis B virus envelope protein required for virion formation. J. Virol. 71 (1997) 9350-9357
6. Chisari F.V., and Ferrari C. Hepatitis B virus immunopathogenesis. Annu. Rev. Immunol. 13 (1995) 29-60
7. Conway J.F., Trus B.L., Booy F.P., Newcomb W.W., Brown J.C., and Steven A.C. Visualization of three-dimensional density maps reconstructed from cryoelectron micrographs of viral capsids. J. Struct. Biol. 116 (1996) 200-208
8. Conway J.F., Cheng N., Zlotnick A., Wingfield P.T., Stahl S.J., and Steven A.C. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 386 (1997) 91-94
9. Conway J.F., Cheng N., Zlotnick A., Stahl S.J., Wingfield P.T., and Steven A.C. Localization of the N terminus of hepatitis B virus capsid protein by peptide-based difference mapping from cryoelectron microscopy. Proc. Natl. Acad. Sci. USA 95 (1998) 14622-14627
10. Craven R.C., and Parent L.J. Dynamic interactions of the Gag polyprotein. Curr. Top. Microbiol. Immunol. 214 (1996) 65-94
11. Crowther R.A., Kiselev N.A., Bottcher B., Berriman J.A., Borisova G.P., Ose V., and Pumpens P. Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy. Cell 77 (1994) 943-950
12. Diminsky D., Schirmbeck R., Reimann J., and Barenholz Y. Comparison between hepatitis B surface antigen (HBsAg) particles derived from mammalian cells (CHO) and yeast cells (Hansenula polymorpha): composition, structure and immunogenicity. Vaccine 15 (1997) 637-647
13. Dryden K.A., Wang G., Yeager M., Nibert M.L., Coombs K.M., Furlong D.B., Fields B.N., and Baker T.S. Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction. J. Cell Biol. 122 (1993) 1023-1041
14. Fisher A.J., and Johnson J.E. Ordered duplex RNA controls capsid architecture in an icosahedral animal virus. Nature 361 (1993) 176-179
15. Ganem D. Hepadnaviridae and their replication. In: Fields B.N., Knipe D.M., Howley P.M., Chanock R.M., Melnick J.L., Monath T.P., Roizman B., and Straus S.E. (Eds). Fields Virology (1996), Lippincott-Raven Publishers, Philadelphia, PA 2703-2737
16. Ganser B.K., Li S., Klishko V.Y., Finch J.T., and Sundquist W.I. Assembly and analysis of conical models for the HIV-1 core. Science 283 (1999) 80-83
17. Gilbert R.J., Beales L., Blond D., Simon M.N., Lin B.Y., Chisari F.V., Stuart D.I., and Rowlands D.J. Hepatitis B small surface antigen particles are octahedral. Proc. Natl. Acad. Sci. USA 102 (2005) 14783-14788
18. Grünewald K., Desai P., Winkler D.C., Heymann J.B., Belnap D.M., Baumeister W., and Steven A.C. Three-dimensional structure of herpes simplex virus from cryo-electron tomography. Science 302 (2003) 1396-1398
19. Guidotti L.G., Martinez V., Loh Y.T., Rogler C.E., and Chisari F.V. Hepatitis B virus nucleocapsid particles do not cross the hepatocyte nuclear membrane in transgenic mice. J. Virol. 68 (1994) 5469-5475
20. Guidotti L.G., Matzke B., Schaller H., and Chisari F.V. High-level hepatitis B virus replication in transgenic mice. J. Virol. 69 (1995) 6158-6169
21. Heymann J.B. Bsoft: image and molecular processing in electron microscopy. J. Struct. Biol. 133 (2001) 156-169
22. Kaplan P.M., Greenman R.L., Gerin J.L., Purcell R.H., and Robinson W.S. DNA polymerase associated with human hepatitis B antigen. J. Virol. 12 (1973) 995-1005
23. Kenney J.M., von Bonsdorff C.H., Nassal M., and Fuller S.D. Evolutionary conservation in the hepatitis B virus core structure: comparison of human and duck cores. Structure 3 (1995) 1009-1019
24. Lambert C., and Prange R. Dual topology of the hepatitis B virus large envelope protein. Determinants influencing post-translational pre-S translocation. J. Biol. Chem. 276 (2001) 22265-22272
25. Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
26. Ponsel D., and Bruss V. Mapping of amino acid side chains on the surface of hepatitis B virus capsids required for envelopment and virion formation. J. Virol. 77 (2003) 416-422
27. Roseman A.M., Berriman J.A., Wynne S.A., Butler P.J., and Crowther R.A. A structural model for maturation of the hepatitis B virus core. Proc. Natl. Acad. Sci. USA 102 (2005) 15821-15826
28. Tihova M., Dryden K.A., Le T.V., Harvey S.C., Johnson J.E., Yeager M., and Schneemann A. Nodavirus coat protein imposes dodecahedral RNA structure independent of nucleotide sequence and length. J. Virol. 78 (2004) 2897-2905
29. Wunderlich G., and Bruss V. Characterization of early hepatitis B virus surface protein oligomers. Arch. Virol. 141 (1996) 1191-1205
30. Wynne S.A., Crowther R.A., and Leslie A.G. The crystal structure of the human hepatitis B virus capsid. Mol. Cell 3 (1999) 771-780
31. Yeager M., Berriman J.A., Baker T.S., and Bellamy A.R. Three-dimensional structure of the rotavirus haemagglutinin VP4 by cryo-electron microscopy and difference map analysis. EMBO J. 13 (1994) 1011-1018
32. Zhang W., Mukhopadhyay S., Pletnev S.V., Baker T.S., Kuhn R.J., and Rossmann M.G. Placement of the structural proteins in Sindbis virus. J. Virol. 76 (2002) 11645-11658
33. Zhou Z.H., Dougherty M., Jakana J., He J., Rixon F.J., and Chiu W. Seeing the herpesvirus capsid at 8.5 Å. Science 288 (2000) 877-880
34. Zlotnick A., Cheng N., Conway J.F., Booy F.P., Steven A.C., Stahl S.J., and Wingfield P.T. Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein. Biochemistry 35 (1996) 7412-7421
35. Zlotnick A., Cheng N., Stahl S.J., Conway J.F., Steven A.C., and Wingfield P.T. Localization of the C terminus of the assembly domain of hepatitis B virus capsid protein: Implications for morphogenesis and organization of encapsidated RNA. Proc. Natl. Acad. Sci. USA 94 (1997) 9556-9561