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Structure of Ljungan virus provides insight into genome packaging of this picornavirus
University of Oxford, UK ; The Pirbright Institute, UK.
Chinese Academy of Science, China.
University of Oxford, UK.
University of Oxford, UK ; The Pirbright Institute, UK.
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2015 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 6, 8316Article in journal (Refereed) Published
Abstract [en]

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-angstrom 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.

Place, publisher, year, edition, pages
2015. Vol. 6, 8316
Keyword [en]
Biological sciences, Biophysics, Virology
National Category
Microbiology
Research subject
Biomedical Sciences, Virology
Identifiers
URN: urn:nbn:se:lnu:diva-47715DOI: 10.1038/ncomms9316ISI: 000364920600001PubMedID: 26446437OAI: oai:DiVA.org:lnu-47715DiVA: diva2:876727
Available from: 2015-12-04 Created: 2015-12-04 Last updated: 2016-10-05Bibliographically approved

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CiteExportLink to record
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Citation style
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