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Journal of Virology, December 2006, p. 11598-11609, Vol. 80, No. 23
0022-538X/06/$08.00+0     doi:10.1128/JVI.01758-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Characterization of White Bream Virus Reveals a Novel Genetic Cluster of Nidoviruses{triangledown}

Heike Schütze,1,2 Rachel Ulferts,3 Barbara Schelle,4 Sonja Bayer,4 Harald Granzow,2 Bernd Hoffmann,5 Thomas C. Mettenleiter,1 and John Ziebuhr3*

Institutes of Molecular Biology,1 Infectology,2 Diagnostic Virology, Friedrich-Loeffler-Institut, 17493 Greifswald-Insel Riems, Germany,5 Centre for Cancer Research and Cell Biology, School of Biomedical Sciences, The Queen's University of Belfast, 97 Lisburn Road, Belfast BT9 7BL, United Kingdom,3 Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany4

Received 14 August 2006/ Accepted 12 September 2006

The order Nidovirales comprises viruses from the families Coronaviridae (genera Coronavirus and Torovirus), Roniviridae (genus Okavirus), and Arteriviridae (genus Arterivirus). In this study, we characterized White bream virus (WBV), a bacilliform plus-strand RNA virus isolated from fish. Analysis of the nucleotide sequence, organization, and expression of the 26.6-kb genome provided conclusive evidence for a phylogenetic relationship between WBV and nidoviruses. The polycistronic genome of WBV contains five open reading frames (ORFs), called ORF1a, -1b, -2, -3, and -4. In WBV-infected cells, three subgenomic RNAs expressing the structural proteins S, M, and N were identified. The subgenomic RNAs were revealed to share a 42-nucleotide, 5' leader sequence that is identical to the 5'-terminal genome sequence. The data suggest that a conserved nonanucleotide sequence, CA(G/A)CACUAC, located downstream of the leader and upstream of the structural protein genes acts as the core transcription-regulating sequence element in WBV. Like other nidoviruses with large genomes (>26 kb), WBV encodes in its ORF1b an extensive set of enzymes, including putative polymerase, helicase, ribose methyltransferase, exoribonuclease, and endoribonuclease activities. ORF1a encodes several membrane domains, a putative ADP-ribose 1"-phosphatase, and a chymotrypsin-like serine protease whose activity was established in this study. Comparative sequence analysis revealed that WBV represents a separate cluster of nidoviruses that significantly diverged from toroviruses and, even more, from coronaviruses, roniviruses, and arteriviruses. The study adds to the amazing diversity of nidoviruses and appeals for a more extensive characterization of nonmammalian nidoviruses to better understand the evolution of these largest known RNA viruses.

* Corresponding author. Mailing address: The Queen's University of Belfast, School of Biomedical Sciences, 97 Lisburn Road, Belfast BT9 7BL, United Kingdom. Phone: 44-28-90972089. Fax: 44-28-90972124. E-mail: j.ziebuhr{at}qub.ac.uk.

{triangledown} Published ahead of print on 20 September 2006.

Journal of Virology, December 2006, p. 11598-11609, Vol. 80, No. 23
0022-538X/06/$08.00+0     doi:10.1128/JVI.01758-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Nedialkova, D. D., Ulferts, R., van den Born, E., Lauber, C., Gorbalenya, A. E., Ziebuhr, J., Snijder, E. J. (2009). Biochemical Characterization of Arterivirus Nonstructural Protein 11 Reveals the Nidovirus-Wide Conservation of a Replicative Endoribonuclease. J. Virol. 83: 5671-5682 [Abstract] [Full Text]  


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