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| Title | Scaffold properties are a key determinant of the size and shape of self-assembled virus-derived particles. |
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| Journal, issue, pages | ACS Chem Biol, Vol. 8, Issue 12, Page 2753-2761, Year 2013 |
| Publish date | Dec 20, 2013 |
 Authors | Stanislav Kler / Joseph Che-Yen Wang / Mary Dhason / Ariella Oppenheim / Adam Zlotnick /  |
| PubMed Abstract | Controlling the geometry of self-assembly will enable a greater diversity of nanoparticles than now available. Viral capsid proteins, one starting point for investigating self-assembly, have evolved ...Controlling the geometry of self-assembly will enable a greater diversity of nanoparticles than now available. Viral capsid proteins, one starting point for investigating self-assembly, have evolved to form regular particles. The polyomavirus SV40 assembles from pentameric subunits and can encapsidate anionic cargos. On short ssRNA (≤814 nt), SV40 pentamers form 22 nm diameter capsids. On RNA too long to fit a T = 1 particle, pentamers forms strings of 22 nm particles and heterogeneous particles of 29-40 nm diameter. However, on dsDNA SV40 forms 50 nm particles composed of 72 pentamers. A 7.2-Å resolution cryo-EM image reconstruction of 22 nm particles shows that they are built of 12 pentamers arranged with T = 1 icosahedral symmetry. At 3-fold vertices, pentamers each contribute to a three-helix triangle. This geometry of interaction is not seen in crystal structures of T = 7 viruses and provides a structural basis for the smaller capsids. We propose that the heterogeneous particles are actually mosaics formed by combining different geometries of interaction from T = 1 capsids and virions. Assembly can be trapped in novel conformations because SV40 interpentamer contacts are relatively strong. The implication is that by virtue of their large catalog of interactions, SV40 pentamers have the ability to self-assemble on and conform to a broad range of shapes. |
 External links | ACS Chem Biol / PubMed:24093474 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 7.2 Å |
| Structure data |  EMDB-2375: |
| Source |
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Xenopus laevis (African clawed frog)