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-Structure paper
| Title | Structure of Ljungan virus provides insight into genome packaging of this picornavirus. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 6, Page 8316, Year 2015 |
| Publish date | Oct 8, 2015 |
 Authors | Ling Zhu / Xiangxi Wang / Jingshan Ren / Claudine Porta / Hannah Wenham / Jens-Ola Ekström / Anusha Panjwani / Nick J Knowles / Abhay Kotecha / C Alistair Siebert / A Michael Lindberg / Elizabeth E Fry / Zihe Rao / Tobias J Tuthill / David I Stuart /    |
| PubMed Abstract | Picornaviruses are responsible for a range of human and animal diseases, but how their RNA genome is packaged remains poorly understood. A particularly poorly studied group within this family are ...Picornaviruses are responsible for a range of human and animal diseases, but how their RNA genome is packaged remains poorly understood. A particularly poorly studied group within this family are those that lack the internal coat protein, VP4. Here we report the atomic structure of one such virus, Ljungan virus, the type member of the genus Parechovirus B, which has been linked to diabetes and myocarditis in humans. The 3.78-Å resolution cryo-electron microscopy structure shows remarkable features, including an extended VP1 C terminus, forming a major protuberance on the outer surface of the virus, and a basic motif at the N terminus of VP3, binding to which orders some 12% of the viral genome. This apparently charge-driven RNA attachment suggests that this branch of the picornaviruses uses a different mechanism of genome encapsidation, perhaps explored early in the evolution of picornaviruses. |
 External links | Nat Commun / PubMed:26446437 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.8 - 4.5 Å |
| Structure data | EMDB-6394, PDB-3jb4:  EMDB-6395: |
| Source |
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 Keywords |  VIRUS / picornaviruses / assembly / pathogen |
