Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Cytoplasmic polyhedrosis virus (CPV) is unique among the double-stranded RNA viruses of the family Reoviridae in having a single capsid layer. Analysis by cryo-electron microscopy allows comparison of the single shelled CPV and orthoreovirus with the high resolution crystal structure of the inner shell of the bluetongue virus (BTV) core. This suggests that the novel arrangement identified in BTV, of 120 protein subunits in a so-called 'T=2' organization, is a characteristic of the Reoviridae and allows us to delineate structural similarities and differences between two subgroups of the family--the turreted and the smooth-core viruses. This in turn suggests a coherent picture of the structural organization of many dsRNA viruses.

Original publication

DOI

10.1038/9347

Type

Journal article

Journal

Nat Struct Biol

Publication Date

06/1999

Volume

6

Pages

565 - 568

Keywords

Bluetongue virus, Capsid, Cryoelectron Microscopy, Crystallization, Genome, Viral, Models, Molecular, Orthoreovirus, Protein Conformation, RNA Viruses, RNA, Double-Stranded, RNA, Viral, Reoviridae, Viral Core Proteins