Abstract
The reovirus core is an assembly with a relative molecular mass of 52 million that synthesizes, modifies and exports viral messenger RNA. Analysis of its structure by X-ray crystallography shows that there are alternative, specific and completely non-equivalent contacts made by several surfaces of two of its proteins; that the RNA capping and export apparatus is a hollow cylinder, which probably sequesters its substrate to ensure completion of the capping reactions; that the genomic double-stranded RNA is coiled into concentric layers within the particle; and that there is a protein shell that appears to be common to all groups of double-stranded RNA viruses.
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Acknowledgements
We thank T. F. Severson, R. L. Margraf and S. J. Harrison for growing reovirus-infected cells; T. S. Baker and S. B. Walker for providing us with an unpublished cryoEM reconstruction of cores from reovirus reassortant F18; D. Thiel and the staff of CHESS and McCHESS and R. Pahl and the staff of the BioCars beamline 14-ID-B for assistance; members of the Harrison laboratory, especially J. Cruzan, for scanning image plates; W. Minor for help with data collected with an early version of the double image plate cassette holder; B. Miller for constructing an improved vacuum-based version; S. Ray for advice on computing strategies; P. Adams and R. Grosse-Kunstleve for advice on refinement; and R. Grosse-Kunstleve for implementing refinement in the smaller rhombohedral cell. K.M.R. thanks D. W. Rodgers for help in the initial cryopreservation attempts, for suggesting a vacuum-based design for the double image plate cassette holder and for advice. We acknowledge support from the NIH (to S.C.H. and M.L.N.). S.C.H. is an investigator in the Howard Hughes Medical Institute. M.L.N. receives support from a grant of the Lucille P. Markey Charitable Trust to the Institute for Molecular Virology and, as a Shaw Scientist, from the Milwaukee Foundation. This work was started with the stimulus and collaboration of the late B. N. Fields.
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Reinisch, K., Nibert, M. & Harrison, S. Structure of the reovirus core at 3.6?Å resolution. Nature 404, 960–967 (2000). https://doi.org/10.1038/35010041
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DOI: https://doi.org/10.1038/35010041
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