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Journal of Virology, November 2005, p. 13385-13398, Vol. 79, No. 21
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.21.13385-13398.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Kelp Fly Virus: a Novel Group of Insect Picorna-Like Viruses as Defined by Genome Sequence Analysis and a Distinctive Virion Structure

C. J. Hartley,1* D. R. Greenwood,2 R. J. C. Gilbert,3,4 A. Masoumi,1 K. H. J. Gordon,1 T. N. Hanzlik,1 E. E. Fry,3 D. I. Stuart,3,4 and P. D. Scotti2

CSIRO Entomology, GPO Box 1700, Acton, ACT 2601, Australia,1 The Horticulture and Food Research Institute of New Zealand, Ltd., 120 Mt. Albert Road, Auckland, New Zealand,2 Division of Structural Biology, Henry Wellcome Building for Genomic Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, United Kingdom,3 Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QH, United Kingdom4

Received 16 March 2005/ Accepted 5 August 2005

The complete genomic sequence of kelp fly virus (KFV), originally isolated from the kelp fly, Chaetocoelopa sydneyensis, has been determined. Analyses of its genomic and structural organization and phylogeny show that it belongs to a hitherto undescribed group within the picorna-like virus superfamily. The single-stranded genomic RNA of KFV is 11,035 nucleotides in length and contains a single large open reading frame encoding a polypeptide of 3,436 amino acids with 5' and 3' untranslated regions of 384 and 343 nucleotides, respectively. The predicted amino acid sequence of the polypeptide shows that it has three regions. The N-terminal region contains sequences homologous to the baculoviral inhibitor of apoptosis repeat domain, an inhibitor of apoptosis commonly found in animals and in viruses with double-stranded DNA genomes. The second region contains at least two capsid proteins. The third region has three sequence motifs characteristic of replicase proteins of many plant and animal viruses, including a helicase, a 3C chymotrypsin-like protease, and an RNA-dependent RNA polymerase. Phylogenetic analysis of the replicase motifs shows that KFV forms a distinct and distant taxon within the picorna-like virus superfamily. Cryoelectron microscopy and image reconstruction of KFV to a resolution of 15 Å reveals an icosahedral structure, with each of its 12 fivefold vertices forming a turret from the otherwise smooth surface of the 20-Å-thick capsid. The architecture of the KFV capsid is unique among the members of the picornavirus superfamily for which structures have previously been determined.

* Corresponding author. Mailing address: CSIRO Entomology, GPO Box 1700, Acton, ACT 2601, Australia. Phone: 61-2-62464159. Fax: 61-2-62464173. E-mail: Carol.Hartley{at}csiro.au.

Journal of Virology, November 2005, p. 13385-13398, Vol. 79, No. 21
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.21.13385-13398.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





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