The complete genome sequence of Shope (rabbit) fibroma virus

Citation
Do. Willer et al., The complete genome sequence of Shope (rabbit) fibroma virus, VIROLOGY, 264(2), 1999, pp. 319-343
Citations number
197
Categorie Soggetti
Microbiology
Journal title
VIROLOGY
ISSN journal
00426822 → ACNP
Volume
264
Issue
2
Year of publication
1999
Pages
319 - 343
Database
ISI
SICI code
0042-6822(19991125)264:2<319:TCGSOS>2.0.ZU;2-8
Abstract
We have determined the complete DNA sequence of the Leporipoxvirus Shope fi broma virus (SFV). The SFV genome spans 159.8 kb and encodes 165 putative g enes of which 13 are duplicated in the 12.4-kb terminal inverted repeats. A lthough most SFV genes have homologs encoded by other Chordopoxvirinae, the SFV genome lacks a key gene required for the production of extracellular e nveloped virus. SFV also encodes only the smaller ribonucleotide reductase subunit and has a limited nucleotide biosynthetic capacity. SFV preserves t he Chordopoxvirinae gene order from S012L near the left end of the chromoso me through to S142R (homologs of vaccinia F2L and B1R, respectively). The u nique right end of SFV appears to be genetically unstable because when the sequence is compared with that of myxoma virus, five myxoma homologs have b een deleted (C. Cameron, S. Hota-Mitchell, L. Chen, J. Barrett, J.-X. Cao, C. Macaulay, D. Willer, D. Evans, and G. McFadden, 1999, Virology 264, 298- 318). Most other differences between these two Leporipoxviruses are located in the telomeres. Leporipoxviruses encode several genes not found in other poxviruses including four small hydrophobic proteins of unknown function ( S023R, S119L, S125R, and S132L), an alpha 2,3-sialyltransferase (S143R), a protein belonging to the Ig-like protein superfamily (S141R), and a protein resembling the DNA-binding domain of proteins belonging to the HIN-200 pro tein family S013L). SFV also encodes a type II DNA photolyase (S127L). Mela noplus sanguinipes entomopoxvirus encodes a similar protein, but SN is the first mammalian virus potentially capable of photoreactivating ultraviolet DNA damage. (C) 1999 Academic Press.