Structure of Ljungan virus provides insight into genome packaging of this picornavirus

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 and David I. Stuart ()
Additional contact information
Ling Zhu: University of Oxford, The Henry Wellcome Building for Genomic Medicine
Xiangxi Wang: National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science
Jingshan Ren: University of Oxford, The Henry Wellcome Building for Genomic Medicine
Claudine Porta: University of Oxford, The Henry Wellcome Building for Genomic Medicine
Hannah Wenham: The Pirbright Institute
Jens-Ola Ekström: Linnaeus University
Anusha Panjwani: The Pirbright Institute
Nick J. Knowles: The Pirbright Institute
Abhay Kotecha: University of Oxford, The Henry Wellcome Building for Genomic Medicine
C. Alistair Siebert: University of Oxford, The Henry Wellcome Building for Genomic Medicine
A. Michael Lindberg: Linnaeus University
Elizabeth E. Fry: University of Oxford, The Henry Wellcome Building for Genomic Medicine
Zihe Rao: National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science
Tobias J. Tuthill: The Pirbright Institute
David I. Stuart: University of Oxford, The Henry Wellcome Building for Genomic Medicine

Nature Communications, 2015, vol. 6, issue 1, 1-9

Abstract: 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 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.

Date: 2015
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DOI: 10.1038/ncomms9316

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