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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.
Vise andre og tillknytning
2015 (engelsk)Inngår i: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 6, artikkel-id 8316Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
2015. Vol. 6, artikkel-id 8316
Emneord [en]
Biological sciences, Biophysics, Virology
HSV kategori
Forskningsprogram
Biomedicinsk vetenskap, Virologi
Identifikatorer
URN: urn:nbn:se:lnu:diva-47715DOI: 10.1038/ncomms9316ISI: 000364920600001PubMedID: 26446437Scopus ID: 2-s2.0-84943631507OAI: oai:DiVA.org:lnu-47715DiVA, id: diva2:876727
Tilgjengelig fra: 2015-12-04 Laget: 2015-12-04 Sist oppdatert: 2017-12-01bibliografisk kontrollert

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