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

• DOI: 10.1038/ncomms9316
• Publication Date: 2015-10-08T09:44:40Z
• 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
• Keywords: Picornavirus; Picornaviridae; RNA virus; Nucleic acid structure; Viral evolution

Abstract Picornaviruses are responsible for a range of human and animal diseases, but how their RNA genome is packaged remains poorly understood. A particularly studied group within this family those that lack the internal coat protein, VP4. Here we report atomic structure one such virus, Ljungan type member genus Parechovirus B, which has been linked to diabetes myocarditis in humans. The 3.78-Å resolution cryo-electron microscopy shows remarkable features, including an extended VP1 C terminus, forming major protuberance on outer surface basic motif at N terminus VP3, binding orders some 12% viral genome. This apparently charge-driven attachment suggests branch picornaviruses uses different mechanism encapsidation, perhaps explored early evolution picornaviruses.