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The crystal structure of cricket paralysis virus: the first view of a new virus family

Nature Structural Biology volume 6, pages 765–774 (1999)Cite this article

Abstract

Numerous small, RNA-containing insect viruses are currently classified as picornaviruses, or as 'picorna-like', since they superficially resemble the true picornaviruses. Considerable evidence now suggests that several of these viruses are members of a distinct family. We have determined the gene sequence of the capsid proteins and the 2.4 Å resolution crystal structure of the cricket paralysis virus. While the genome sequence indicates that the insect picorna-like viruses represent a distinct lineage compared to true picornaviruses, the capsid structure demonstrates that the two groups are related. These viral genomes are, thus, best viewed as composed of exchangeable modules that have recombined.

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Figure 1: a, The organization of a standard picornavirus genome, with the structural proteins (encoded in the P1 segment) at the 5' end.
Figure 2: The amino acid sequences of the capsid proteins from CrPV.
Figure 3: A stereoview of the electron density surrounding residues 2,228 to 2,232 (from strand βI), from the final 2.4 Å map.
Figure 4: a, The structure of the CrPV protomer (that is, the subunit comprising a single polypeptide chain prior to cleavage into the four subunits).
Figure 5: a, A space-filling representation of a single pentamer of poliovirus, showing the characteristic surface features of the canyon and 5-fold crest.
Figure 6: The interactions of the capsid proteins around the icosahedral 2-fold axis, seen from the inside of the capsid, looking towards the exterior.
Figure 7: The interactions of VP4 around the 5-fold axis, seen from the outside of the capsid looking towards the center of the particle.

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Acknowledgements

We would like to thank F. Weyts, K. Johnson, A. Claudianos, A.-M. Wilkes and N. Gibb for their assistance with cloning and sequencing of the CrPV genome; S. Dearing and P. Hoefakker for assistance with the production of CrPV; V. Reddy, X.F. Dong and A. Kumar for their help in data collection; H. Giesing for comments and discussions; and B. Sheehan for assistance with computing and figures for this manuscript. Data were collected on beamline F-1 of the Cornell High Energy Synchrotron Source (CHESS), with time awarded through CHESS proposal 205. This work was supported by funding from the National Institutes of Health.

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  1. John Tate

    Present address: San Diego Supercomputer Center, University of California, 9500 Gilman Drive, San Diego, La Jolla, California, 92093-0505, USA

Authors and Affiliations

  1. Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla , 92037, California, USA

    John Tate, Lars Liljas, Tianwei Lin & John E. Johnson

  2. Department of Molecular Biology, University of Uppsala, Uppsala, Sweden

    Lars Liljas

  3. The Horticulture and Food Research Institute of New Zealand Ltd., Mt. Albert Research Centre, Private Bag 92169 , Auckland, New Zealand

    Paul Scotti

  4. CSIRO Division of Entomology, GPO Box 1700, Canberra, 2601, Australia

    Peter Christian

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Correspondence to John E. Johnson.

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Tate, J., Liljas, L., Scotti, P. et al. The crystal structure of cricket paralysis virus: the first view of a new virus family. Nat Struct Mol Biol 6, 765–774 (1999). https://doi.org/10.1038/11543

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