publication . Article . Other literature type . 2015

Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM

Rebecca Thompson; Neil Ranson; Joseph Cockburn;
Open Access English
  • Published: 10 Dec 2015 Journal: Nature Communications, volume 6 (eissn: 2041-1723, Copyright policy)
  • Publisher: Nature Publishing Group
  • Country: United Kingdom
Abstract
Cowpea mosaic virus is a plant-infecting member of the Picornavirales and is of major interest in the development of biotechnology applications. Despite the availability of >100 crystal structures of Picornavirales capsids, relatively little is known about the mechanisms of capsid assembly and genome encapsidation. Here we have determined cryo-electron microscopy reconstructions for the wild-type virus and an empty virus-like particle, to 3.4 Å and 3.0 Å resolution, respectively, and built de novo atomic models of their capsids. These new structures reveal the C-terminal region of the small coat protein subunit, which is essential for virus assembly and which wa...
Subjects
Medical Subject Headings: viruses
free text keywords: Article, General Biochemistry, Genetics and Molecular Biology, General Physics and Astronomy, General Chemistry
Funded by
WT| New infrastructure for EM studies at the University of Leeds.
Project
  • Funder: Wellcome Trust (WT)
  • Project Code: 090932
  • Funding stream: Cellular and Molecular Neuroscience
,
RCUK| Untangling the processes of replication and encapsidation in Picornavirales
Project
  • Funder: Research Council UK (RCUK)
  • Project Code: BB/L020955/1
  • Funding stream: BBSRC
,
WT| The Structural Basis of Biological Mechanisms
Project
  • Funder: Wellcome Trust (WT)
  • Project Code: 096685
  • Funding stream: Cellular and Molecular Neuroscience
,
WT| The molecular basis of biological mechanisms
Project
  • Funder: Wellcome Trust (WT)
  • Project Code: 086774
  • Funding stream: Cellular and Molecular Neuroscience
,
WT| Structural Molecular Biology Infrastructure for the Astbury Centre at Leeds.
Project
  • Funder: Wellcome Trust (WT)
  • Project Code: 094232
  • Funding stream: Cellular and Molecular Neuroscience
51 references, page 1 of 4

1. Natarajan, P. et al. Exploring icosahedral virus structures with VIPER. Nat. Rev. Microbiol. 3, 809-817 (2005).

2. Jiang, P., Liu, Y., Ma, H.-C., Paul, A. V. & Wimmer, E. Picornavirus morphogenesis. Microbiol. Mol. Biol. Rev. 78, 418-437 (2014).

3. Lin, T. & Johnson, J. E. Structures of picorna-like plant viruses: implications and applications. Adv. Virus Res. 62, 167-239 (2003).

4. Lin, T. et al. The refined crystal structure of cowpea mosaic virus at 2.8 Å resolution. Virology 265, 20-34 (1999).

5. Ochoa, W. F., Chatterji, A., Lin, T. & Johnson, J. E. Generation and structural analysis of reactive empty particles derived from an icosahedral virus. Chem. Biol. 13, 771-778 (2006).

6. Chen, Z. G. et al. Protein-RNA interactions in an icosahedral virus at 3.0 Å resolution. Science 245, 154-159 (1989).

7. Lin, T. et al. Structural fingerprinting: subgrouping of comoviruses by structural studies of red clover mottle virus to 2.4 Å resolution and comparisons with other comoviruses. J. Virol. 74, 493-504 (2000).

8. MacFarlane, S. A., Shanks, M., Davies, J. W., Zlotnick, A. & Lomonossoff, G. P. Analysis of the nucleotide sequence of bean pod mottle virus middle component RNA. Virology 183, 405-409 (1991). [OpenAIRE]

9. Taylor, K. M., Spall, V. E., Butler, P. J. & Lomonossoff, G. P. The cleavable carboxyl terminus of the small coat protein of cowpea mosaic virus is involved in RNA encapsidation. Virology 255, 129-137 (1999). [OpenAIRE]

10. Lomonossoff, G. P. & Johnson, J. E. The synthesis and structure of comovirus capsids. Prog. Biophys. Mol. Biol. 55, 107-137 (1991).

11. Can˜izares, M. C., Taylor, K. M. & Lomonossoff, G. P. Surface-exposed C-terminal amino acids of the small coat protein of Cowpea mosaic virus are required for suppression of silencing. J. Gen. Virol. 85, 3431-3435 (2004).

12. Saunders, K., Sainsbury, F. & Lomonossoff, G. P. Efficient generation of cowpea mosaic virus empty virus-like particles by the proteolytic processing of precursors in insect cells and plants. Virology 393, 329-337 (2009).

13. Sainsbury, F., Saunders, K., Aljabali, A. A. A., Evans, D. J. & Lomonossoff, G. P. Peptide-controlled access to the interior surface of empty virus nanoparticles. Chembiochem. 12, 2435-2440 (2011).

14. Steinmetz, N. F., Lin, T., Lomonossoff, G. P. & Johnson, J. E. Structure-based engineering of an icosahedral virus for nanomedicine and nanotechnology. Curr. Top. Microbiol. Immunol. 327, 23-58 (2009).

15. Montague, N. P. et al. Recent advances of Cowpea mosaic virus-based particle technology. Hum. Vaccin. 7, 383-390 (2011).

51 references, page 1 of 4
Abstract
Cowpea mosaic virus is a plant-infecting member of the Picornavirales and is of major interest in the development of biotechnology applications. Despite the availability of >100 crystal structures of Picornavirales capsids, relatively little is known about the mechanisms of capsid assembly and genome encapsidation. Here we have determined cryo-electron microscopy reconstructions for the wild-type virus and an empty virus-like particle, to 3.4 Å and 3.0 Å resolution, respectively, and built de novo atomic models of their capsids. These new structures reveal the C-terminal region of the small coat protein subunit, which is essential for virus assembly and which wa...
Subjects
Medical Subject Headings: viruses
free text keywords: Article, General Biochemistry, Genetics and Molecular Biology, General Physics and Astronomy, General Chemistry
Funded by
WT| New infrastructure for EM studies at the University of Leeds.
Project
  • Funder: Wellcome Trust (WT)
  • Project Code: 090932
  • Funding stream: Cellular and Molecular Neuroscience
,
RCUK| Untangling the processes of replication and encapsidation in Picornavirales
Project
  • Funder: Research Council UK (RCUK)
  • Project Code: BB/L020955/1
  • Funding stream: BBSRC
,
WT| The Structural Basis of Biological Mechanisms
Project
  • Funder: Wellcome Trust (WT)
  • Project Code: 096685
  • Funding stream: Cellular and Molecular Neuroscience
,
WT| The molecular basis of biological mechanisms
Project
  • Funder: Wellcome Trust (WT)
  • Project Code: 086774
  • Funding stream: Cellular and Molecular Neuroscience
,
WT| Structural Molecular Biology Infrastructure for the Astbury Centre at Leeds.
Project
  • Funder: Wellcome Trust (WT)
  • Project Code: 094232
  • Funding stream: Cellular and Molecular Neuroscience
51 references, page 1 of 4

1. Natarajan, P. et al. Exploring icosahedral virus structures with VIPER. Nat. Rev. Microbiol. 3, 809-817 (2005).

2. Jiang, P., Liu, Y., Ma, H.-C., Paul, A. V. & Wimmer, E. Picornavirus morphogenesis. Microbiol. Mol. Biol. Rev. 78, 418-437 (2014).

3. Lin, T. & Johnson, J. E. Structures of picorna-like plant viruses: implications and applications. Adv. Virus Res. 62, 167-239 (2003).

4. Lin, T. et al. The refined crystal structure of cowpea mosaic virus at 2.8 Å resolution. Virology 265, 20-34 (1999).

5. Ochoa, W. F., Chatterji, A., Lin, T. & Johnson, J. E. Generation and structural analysis of reactive empty particles derived from an icosahedral virus. Chem. Biol. 13, 771-778 (2006).

6. Chen, Z. G. et al. Protein-RNA interactions in an icosahedral virus at 3.0 Å resolution. Science 245, 154-159 (1989).

7. Lin, T. et al. Structural fingerprinting: subgrouping of comoviruses by structural studies of red clover mottle virus to 2.4 Å resolution and comparisons with other comoviruses. J. Virol. 74, 493-504 (2000).

8. MacFarlane, S. A., Shanks, M., Davies, J. W., Zlotnick, A. & Lomonossoff, G. P. Analysis of the nucleotide sequence of bean pod mottle virus middle component RNA. Virology 183, 405-409 (1991). [OpenAIRE]

9. Taylor, K. M., Spall, V. E., Butler, P. J. & Lomonossoff, G. P. The cleavable carboxyl terminus of the small coat protein of cowpea mosaic virus is involved in RNA encapsidation. Virology 255, 129-137 (1999). [OpenAIRE]

10. Lomonossoff, G. P. & Johnson, J. E. The synthesis and structure of comovirus capsids. Prog. Biophys. Mol. Biol. 55, 107-137 (1991).

11. Can˜izares, M. C., Taylor, K. M. & Lomonossoff, G. P. Surface-exposed C-terminal amino acids of the small coat protein of Cowpea mosaic virus are required for suppression of silencing. J. Gen. Virol. 85, 3431-3435 (2004).

12. Saunders, K., Sainsbury, F. & Lomonossoff, G. P. Efficient generation of cowpea mosaic virus empty virus-like particles by the proteolytic processing of precursors in insect cells and plants. Virology 393, 329-337 (2009).

13. Sainsbury, F., Saunders, K., Aljabali, A. A. A., Evans, D. J. & Lomonossoff, G. P. Peptide-controlled access to the interior surface of empty virus nanoparticles. Chembiochem. 12, 2435-2440 (2011).

14. Steinmetz, N. F., Lin, T., Lomonossoff, G. P. & Johnson, J. E. Structure-based engineering of an icosahedral virus for nanomedicine and nanotechnology. Curr. Top. Microbiol. Immunol. 327, 23-58 (2009).

15. Montague, N. P. et al. Recent advances of Cowpea mosaic virus-based particle technology. Hum. Vaccin. 7, 383-390 (2011).

51 references, page 1 of 4
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