Key result
Cryo-EM structure of Ljungan virus reveals a VP3 motif binding 12% of the viral genome.
Why the study?
The mechanism of RNA genome packaging in picornaviruses, especially those lacking the internal coat protein VP4, remains poorly understood.
Population
Ljungan virus, type member of genus Parechovirus B
Design
Cryo-electron microscopy structure determination
Authors
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Reveals atomic details of VP4-lacking picornavirus; extends genome-packaging models but leaves myocarditis links hypothesis-generating.
The atomic structure of Ljungan virus reveals a charge-driven RNA attachment mechanism for genome encapsidation, providing insight into the assembly of picornaviruses lacking the VP4 protein.
Zhu et al. (2015) studied Ljungan virus. The 3.78-Å resolution cryo-electron microscopy structure of Ljungan virus reveals an extended VP1 C terminus and a basic motif at the N terminus of VP3 that binds and orders 12% of the viral genome.
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