publication . Article . Other literature type . 2016

Crystal Structure and Proteomics Analysis of Empty Virus-like Particles of Cowpea Mosaic Virus.

Neil Ranson;
Open Access
  • Published: 05 Apr 2016
  • Country: United Kingdom
Abstract
Empty virus-like particles (eVLPs) of Cowpea mosaic virus (CPMV) are currently being utilized as reagents in various biomedical and nanotechnology applications. Here, we report the crystal structure of CPMV eVLPs determined using X-ray crystallography at 2.3 A resolution and compare it with previously reported cryo-electron microscopy (cryo-EM) of eVLPs and virion crystal structures. Although the X-ray and cryo-EM structures of eVLPs are mostly similar, there exist significant differences at the C terminus of the small (S) subunit. The intact C terminus of the S subunit plays a critical role in enabling the efficient assembly of CPMV virions and eVLPs, but under...
Subjects
Medical Subject Headings: viruses
free text keywords: Article, Molecular Biology, Structural Biology
Funded by
NIH| X-ray diffraction analysis of human adenoviruses
Project
  • Funder: National Institutes of Health (NIH)
  • Project Code: 5R01AI070771-06
  • Funding stream: NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES

Aljabali, A.A., Barclay, J.E., Butt, J.N., Lomonossoff, G.P., and Evans, D.J. (2010). Redox-active ferrocene-modified Cowpea mosaic virus nanoparticles. Dalton Trans 39, 7569-7574. [OpenAIRE]

Aljabali, A.A., Barclay, J.E., Steinmetz, N.F., Lomonossoff, G.P., and Evans, D.J. (2012).

Controlled immobilisation of active enzymes on the cowpea mosaic virus capsid. Nanoscale 4, 5640-5645.

Aljabali, A.A., Shah, S.N., Evans-Gowing, R., Lomonossoff, G.P., and Evans, D.J. (2011).

Chemically-coupled-peptide-promoted virus nanoparticle templated mineralization. Integr Biol (Camb) 3, 119-125.

Aljabali, A.A., Shukla, S., Lomonossoff, G.P., Steinmetz, N.F., and Evans, D.J. (2013). CPMVDOX delivers. Mol Pharm 10, 3-10.

Brunger, A.T. (1992). X-PLOR, version 3.1: A system for X-ray crystallography and NMR (New Haven, Connecticut: Yale Univ. Press).

Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., et al. (1998). Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54, 905-921.

Buchan, D.W., Minneci, F., Nugent, T.C., Bryson, K., and Jones, D.T. (2013). Scalable web services for the PSIPRED Protein Analysis Workbench. Nucleic Acids Res 41, W349-357. [OpenAIRE]

Canizares, M.C., Taylor, K.M., and Lomonossoff, G.P. (2004). 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. [OpenAIRE]

CCP4. (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50, 760-763.

Cowtan, K. (2008). Fitting molecular fragments into electron density. Acta Crystallogr D Biol Crystallogr 64, 83-89. [OpenAIRE]

Dalsgaard, K., Uttenthal, A., Jones, T.D., Xu, F., Merryweather, A., Hamilton, W.D., Langeveld, J.P., Boshuizen, R.S., Kamstrup, S., Lomonossoff, G.P., et al. (1997). Plant-derived vaccine protects target animals against a viral disease. Nat Biotechnol 15, 248-252. [OpenAIRE]

Abstract
Empty virus-like particles (eVLPs) of Cowpea mosaic virus (CPMV) are currently being utilized as reagents in various biomedical and nanotechnology applications. Here, we report the crystal structure of CPMV eVLPs determined using X-ray crystallography at 2.3 A resolution and compare it with previously reported cryo-electron microscopy (cryo-EM) of eVLPs and virion crystal structures. Although the X-ray and cryo-EM structures of eVLPs are mostly similar, there exist significant differences at the C terminus of the small (S) subunit. The intact C terminus of the S subunit plays a critical role in enabling the efficient assembly of CPMV virions and eVLPs, but under...
Subjects
Medical Subject Headings: viruses
free text keywords: Article, Molecular Biology, Structural Biology
Funded by
NIH| X-ray diffraction analysis of human adenoviruses
Project
  • Funder: National Institutes of Health (NIH)
  • Project Code: 5R01AI070771-06
  • Funding stream: NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES

Aljabali, A.A., Barclay, J.E., Butt, J.N., Lomonossoff, G.P., and Evans, D.J. (2010). Redox-active ferrocene-modified Cowpea mosaic virus nanoparticles. Dalton Trans 39, 7569-7574. [OpenAIRE]

Aljabali, A.A., Barclay, J.E., Steinmetz, N.F., Lomonossoff, G.P., and Evans, D.J. (2012).

Controlled immobilisation of active enzymes on the cowpea mosaic virus capsid. Nanoscale 4, 5640-5645.

Aljabali, A.A., Shah, S.N., Evans-Gowing, R., Lomonossoff, G.P., and Evans, D.J. (2011).

Chemically-coupled-peptide-promoted virus nanoparticle templated mineralization. Integr Biol (Camb) 3, 119-125.

Aljabali, A.A., Shukla, S., Lomonossoff, G.P., Steinmetz, N.F., and Evans, D.J. (2013). CPMVDOX delivers. Mol Pharm 10, 3-10.

Brunger, A.T. (1992). X-PLOR, version 3.1: A system for X-ray crystallography and NMR (New Haven, Connecticut: Yale Univ. Press).

Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., et al. (1998). Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54, 905-921.

Buchan, D.W., Minneci, F., Nugent, T.C., Bryson, K., and Jones, D.T. (2013). Scalable web services for the PSIPRED Protein Analysis Workbench. Nucleic Acids Res 41, W349-357. [OpenAIRE]

Canizares, M.C., Taylor, K.M., and Lomonossoff, G.P. (2004). 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. [OpenAIRE]

CCP4. (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50, 760-763.

Cowtan, K. (2008). Fitting molecular fragments into electron density. Acta Crystallogr D Biol Crystallogr 64, 83-89. [OpenAIRE]

Dalsgaard, K., Uttenthal, A., Jones, T.D., Xu, F., Merryweather, A., Hamilton, W.D., Langeveld, J.P., Boshuizen, R.S., Kamstrup, S., Lomonossoff, G.P., et al. (1997). Plant-derived vaccine protects target animals against a viral disease. Nat Biotechnol 15, 248-252. [OpenAIRE]

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