Sequence of genome segment 9 of bluetongue virus (serotype 1, South Africa) and expression analysis demonstrating that different forms of VP6 are derived from initiation of protein synthesis at two distinct sites

Wade-Evans, A.M.; Mertens, Peter P. C.; Belsham, Graham J.

doi:10.1099/0022-1317-73-11-3023

Cited by 18 publications

(9 citation statements)

References 22 publications

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“…Of the 112 BTV strains analysed, 96 isolates had two in frame initiation codons, at nucleotides 16 to 18 and 28 to 30 of Seg-9, which can generate two related forms of VP6. This agrees with previous observations of two closely migrating VP6 bands in purified BTV particles or in in vitro translation studies [86]. Only 16 isolates (belonging to both eastern and western topotypes) had a single start codon at nucleotides 28 to 30.…”

Section: Resultssupporting

confidence: 92%

Full Genome Characterisation of Bluetongue Virus Serotype 6 from the Netherlands 2008 and Comparison to Other Field and Vaccine Strains

Maan

Rijn³

et al. 2010

PLoS ONE

126

239

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In mid September 2008, clinical signs of bluetongue (particularly coronitis) were observed in cows on three different farms in eastern Netherlands (Luttenberg, Heeten, and Barchem), two of which had been vaccinated with an inactivated BTV-8 vaccine (during May-June 2008). Bluetongue virus (BTV) infection was also detected on a fourth farm (Oldenzaal) in the same area while testing for export. BTV RNA was subsequently identified by real time RT-PCR targeting genome-segment (Seg-) 10, in blood samples from each farm. The virus was isolated from the Heeten sample (IAH “dsRNA virus reference collection” [dsRNA-VRC] isolate number NET2008/05) and typed as BTV-6 by RT-PCR targeting Seg-2. Sequencing confirmed the virus type, showing an identical Seg-2 sequence to that of the South African BTV-6 live-vaccine-strain. Although most of the other genome segments also showed very high levels of identity to the BTV-6 vaccine (99.7 to 100%), Seg-10 showed greatest identity (98.4%) to the BTV-2 vaccine (RSAvvv2/02), indicating that NET2008/05 had acquired a different Seg-10 by reassortment. Although Seg-7 from NET2008/05 was also most closely related to the BTV-6 vaccine (99.7/100% nt/aa identity), the Seg-7 sequence derived from the blood sample of the same animal (NET2008/06) was identical to that of the Netherlands BTV-8 (NET2006/04 and NET2007/01). This indicates that the blood contained two different Seg-7 sequences, one of which (from the BTV-6 vaccine) was selected during virus isolation in cell-culture. The predominance of the BTV-8 Seg-7 in the blood sample suggests that the virus was in the process of reassorting with the northern field strain of BTV-8. Two genome segments of the virus showed significant differences from the BTV-6 vaccine, indicating that they had been acquired by reassortment event with BTV-8, and another unknown parental-strain. However, the route by which BTV-6 and BTV-8 entered northern Europe was not established.

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Section: Resultssupporting

confidence: 92%

Full Genome Characterisation of Bluetongue Virus Serotype 6 from the Netherlands 2008 and Comparison to Other Field and Vaccine Strains

Maan

Rijn³

et al. 2010

PLoS ONE

126

239

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“…1). Furthermore, a similar situation has been reported for bluetongue virus protein VP6 (48); the two closely migrating forms of this protein are the result of initiation of protein synthesis at two distinct sites and not of posttranslational modification (48). Future work in our laboratory will address these questions.…”

Section: Discussionsupporting

confidence: 66%

Intracellular posttranslational modifications of S1133 avian reovirus proteins

Varela

Martı́nez-Costas

Mallo

et al. 1996

J Virol

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Avian reovirus S1133 specifies at least 10 primary translation products, eight of which are present in the viral particle and two of which are nonstructural proteins. In the work presented here, we studied the covalent modifications undergone by these translation products in the infected cell. The structural polypeptide 2 was shown to be intracellularly modified by both myristoylation and proteolysis. The site-specific cleavage of 2 yielded a large carboxy-terminal fragment and a myristoylated ϳ5,500-M r peptide corresponding to the amino terminus. Both 2 and its cleavage products were found to be structural components of the reovirion. Most avian reovirus proteins were found to be glycosylated and to have a blocking group at the amino terminus. In contrast to the mammalian reovirus system, none of the avian reovirus polypeptides was found to incorporate phosphorus during infection. Our results add to current understanding of the similarities and differences between avian and mammalian reoviruses.Avian reoviruses are very similar in structure and molecular composition to mammalian reoviruses. Both groups have a genome consisting of 10 segments of double-stranded RNA surrounded by a two-layer capsid which also encloses a number of short oligonucleotides (13). However, avian reoviruses differ from their mammalian counterparts in lacking hemagglutinating activity (11) and in being able to induce fusion of cultured cells (27).Mammalian reovirus type 3, the prototype of the genus Orthoreovirus, encodes 11 primary translation products which can be separated into three size classes: large (), medium (), and small () (38). The viral polypeptide 1, encoded by the M2 genomic segment, is proteolytically cleaved in the infected cell to yield 1C and 1N, the latter being a small peptide that corresponds to the amino terminus of the precursor. All three polypeptides are structural components of the virion (30). Intracellular covalent modifications of mammalian reovirus proteins have also been documented. Specifically, 1 and 1N contain an amide-linked myristoyl group attached to their amino-terminal glycines (30), and the presence of this group is necessary for the subsequent site-specific cleavage of 1 to 1C in transfected COS cells (43). There is also evidence for the presence of phosphoserine residues in 1C (16), and both 1 and 1C have been shown to be polyadenylylated and/or ADP-ribosylated (3,4). The presence of glycoproteins in mammalian reovirions was first suggested by the fact that treatment of purified virions with ␤-glycosidase, potassium periodate, sodium borohydride, or lysozyme reduced both the hemagglutination titer and the infectivity of the virus (19,20,42). However, subsequent work on the glycosylation of mammalian reovirus proteins has produced conflicting results: Krystal et al. reported (15) that 1C was the only polypeptide glycosylated, whereas the results of Lee (18) suggested that all mammalian reovirus polypeptides except 2 are glycoproteins. As far as we are aware, there have been no subsequent attempts...

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“…Several genome segments of other reoviruses and other orbiviruses also have weak or moderate Kozak sequence but still appear to be translated effectively in infected cells [28], [31]. Previous studies have also identified more than one initiation codons near the upstream terminus of BTV Seg-9 and Seg-10, both of which appear to be functional, generating multiple related proteins in infected cells [2], [35], [36], [37], [38]. However, it is unclear if more than one protein is translated from Seg-2 or Seg-5 of UMAV.…”

Section: Resultsmentioning

confidence: 99%

Umatilla Virus Genome Sequencing and Phylogenetic Analysis: Identification of Stretch Lagoon Orbivirus as a New Member of the Umatilla virus Species

Belaganahalli

Maan

et al. 2011

PLoS ONE

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The genus Orbivirus, family Reoviridae, includes 22 species of viruses with genomes composed of ten segments of linear dsRNA that are transmitted between their vertebrate hosts by insects or ticks, or with no identified vectors. Full-genome sequence data are available for representative isolates of the insect borne mammalian orbiviruses (including bluetongue virus), as well as a tick borne avian orbivirus (Great Island virus). However, no sequence data are as yet available for the mosquito borne avian orbiviruses.We report full-length, whole-genome sequence data for Umatilla virus (UMAV), a mosquito borne avian orbivirus from the USA, which belongs to the species Umatilla virus. Comparisons of conserved genome segments 1, 2 and 8 (Seg-1, Seg-2 and Seg-8) - encoding the polymerase-VP1, sub-core ‘T2’ protein and core-surface ‘T13’ protein, respectively, show that UMAV groups with the mosquito transmitted mammalian orbiviruses. The highest levels of sequence identity were detected between UMAV and Stretch Lagoon orbivirus (SLOV) from Australia, showing that they belong to the same virus species (with nt/aa identity of 76.04%/88.07% and 77.96%/95.36% in the polymerase and T2 genes and protein, respectively). The data presented here has assisted in identifying the SLOV as a member of the Umatilla serogroup. This sequence data reported here will also facilitate identification of new isolates, and epidemiological studies of viruses belonging to the species Umatilla virus.

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Sequence of genome segment 9 of bluetongue virus (serotype 1, South Africa) and expression analysis demonstrating that different forms of VP6 are derived from initiation of protein synthesis at two distinct sites

Cited by 18 publications

References 22 publications

Full Genome Characterisation of Bluetongue Virus Serotype 6 from the Netherlands 2008 and Comparison to Other Field and Vaccine Strains

Full Genome Characterisation of Bluetongue Virus Serotype 6 from the Netherlands 2008 and Comparison to Other Field and Vaccine Strains

Intracellular posttranslational modifications of S1133 avian reovirus proteins

Umatilla Virus Genome Sequencing and Phylogenetic Analysis: Identification of Stretch Lagoon Orbivirus as a New Member of the Umatilla virus Species

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