1887

Abstract

The simian virus 40 (SV40) capsid is composed of 72 pentamers of VP1, the major protein of SV40. These pentamers are arranged in a =7 icosahedral surface lattice, which is maintained by three types of appropriately arranged, non-equivalent interactions between the pentamers. However, it remains unclear how these interactions are achieved. In this study, the assembly of recombinant VP1 was analysed. Electron microscopy observations revealed that these recombinant VP1 proteins assembled into structurally polymorphic particles depending on environmental conditions. VP1 pentamers assembled efficiently into virus-like particles (VLPs) when high concentrations of ammonium sulfate were present. However, in the presence of 1 M NaCl and 2 mM CaCl at neutral pH, VP1 pentamers formed not only VLPs but also produced tiny =1 icosahedral particles and tubular structures. The exclusion of CaCl resulted in the exclusive formation of tiny particles. In contrast, in the presence of 150 mM NaCl at pH 5, the VP1 pentamers produced only extraordinarily long tubular structures. VP1 is thus quite unique in that it can assemble into such diverse structures. These observations provide clues that will help elucidate the mechanisms underlying SV40 capsid formation.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/vir.0.19067-0
2003-07-01
2020-08-03
Loading full text...

Full text loading...

/deliver/fulltext/jgv/84/7/vir841899.html?itemId=/content/journal/jgv/10.1099/vir.0.19067-0&mimeType=html&fmt=ahah

References

  1. Anderer F. A., Schlumberger H. D., Koch M. A., Frank H., Eggers H. J.. 1967; Structure of simian virus 40. II. Symmetry and components of the virus particle. Virology32:511–523
    [Google Scholar]
  2. Baker T. S., Caspar D. L., Murakami W. T.. 1983; Polyoma virus ‘hexamer’ tubes consist of paired pentamers. Nature303:446–448
    [Google Scholar]
  3. Brady J. N., Winston V. D., Consigli R. A.. 1977; Dissociation of polyoma virus by the chelation of calcium ions found associated with purified virions. J Virol23:717–724
    [Google Scholar]
  4. Brady J. N., Winston V. D., Consigli R. A.. 1978; Characterization of a DNA–protein complex and capsomere subunits derived from polyoma virus by treatment with ethyleneglycol-bis- N , N ′-tetraacetic acid and dithiothreitol. J Virol27:193–204
    [Google Scholar]
  5. Brady J. N., Kendall J. D., Consigli R. A.. 1979; In vitro reassembly of infectious polyoma virions. J Virol32:640–647
    [Google Scholar]
  6. Chang D., Fung C. Y., Ou W. C., Chao P. C., Li S. Y., Wang M., Huang Y. L., Tzeng T. Y., Tsai R. T.. 1997; Self-assembly of the JC virus major capsid protein, VP1, expressed in insect cells. J Gen Virol78:1435–1439
    [Google Scholar]
  7. Colomar M. C., Degoumois-Sahli C., Beard P.. 1993; Opening and refolding of simian virus 40 and in vitro packaging of foreign DNA. J Virol67:2779–2786
    [Google Scholar]
  8. Forstova J., Krauzewicz N., Wallace S., Street A. J., Dilworth S. M., Beard S., Griffin B. E.. 1993; Cooperation of structural proteins during late events in the life cycle of polyomavirus. J Virol67:1405–1413
    [Google Scholar]
  9. Gillock E. T., Rottinghaus S., Chang D., Cai X., Smiley S. A., An K., Consigli R. A.. 1997; Polyomavirus major capsid protein VP1 is capable of packaging cellular DNA when expressed in the baculovirus system. J Virol71:2857–2865
    [Google Scholar]
  10. Ishizu K. I., Watanabe H., Han S. I., Kanesashi S. N., Hoque M., Yajima H., Kataoka K., Handa H.. 2001; Roles of disulfide linkage and calcium ion-mediated interactions in assembly and disassembly of virus-like particles composed of simian virus 40 VP1 capsid protein. J Virol75:61–72
    [Google Scholar]
  11. Koch M. A., Eggers H. J., Anderer F. A., Schlumberger H. D., Frank H.. 1967; Structure of simian virus 40. I. Purification and physical characterization of the virus particle. Virology32:503–510
    [Google Scholar]
  12. Kosukegawa A., Arisaka F., Takayama M., Yajima H., Kaidow A., Handa H.. 1996; Purification and characterization of virus-like particles and pentamers produced by the expression of SV40 capsid proteins in insect cells. Biochim Biophys Acta1290:37–45
    [Google Scholar]
  13. Liddington R. C., Yan Y., Moulai J., Sahli R., Benjamin T. L., Harrison S. C.. 1991; Structure of simian virus 40 at 3·8-Å resolution. Nature354:278–284
    [Google Scholar]
  14. Montross L., Watkins S., Moreland R. B., Mamon H., Caspar D. L. D., Garcea R. L.. 1991; Nuclear assembly of polyomavirus capsids in insect cells expressing the major capsid protein VP1. J Virol65:4991–4998
    [Google Scholar]
  15. Rayment I., Baker T. S., Caspar D. L. D., Murakami W. T.. 1982; Polyoma virus capsid structure at 22·5 Å resolution. Nature295:110–115
    [Google Scholar]
  16. Salunke D. M., Caspar D. L., Garcea R. L.. 1986; Self-assembly of purified polyomavirus capsid protein VP1. Cell46:895–904
    [Google Scholar]
  17. Salunke D. M., Caspar D. L., Garcea R. L.. 1989; Polymorphism in the assembly of polyomavirus capsid protein VP1. Biophys J56:887–900
    [Google Scholar]
  18. Stehle T., Gamblin S. J., Yan Y., Harrison S. C.. 1996; The structure of simian virus 40 refined at 3·1 Å resolution. Structure4:165–182
    [Google Scholar]
  19. Strayer D. S.. 1999; Gene therapy using SV40-derived vectors: what does the future hold?. J Cell Physiol181:375–384
    [Google Scholar]
  20. Yan Y., Stehle T., Liddington R. C., Zhao H., Harrison S. C.. 1996; Structure determination of simian virus 40 and murine polyomavirus by a combination of 30-fold and 5-fold electron-density averaging. Structure4:157–164
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/vir.0.19067-0
Loading
/content/journal/jgv/10.1099/vir.0.19067-0
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error