Bluetongue virus

Canada Minister of National Health and Welfare. Laboratory Centre for Disease Control, Office of Biosafety. Material Safety Data Sheet-Infectious Substances Bluetongue Virus. January 23, 2001. 

Diprose, J. M., et al. (2001). Translocation portals for the substrates and products of a viral transcription complex the bluetongue virus core. EMBO. 20, 7229-7239. 

Gouet, R, et al. (1999). The highly ordered double-stranded RNA genome of bluetongue virus revealed by crystallography. Cell 97,481 90. 

Hewat, E. A., Booth, T. F. and Roy, R (1994). Structure of correctly self-assembled bluetongue virus-like particles. /. Struct. Biol. 112,183-191. 

Taking into account process integration, i.e. - cultivation and product purification, particle locaHsation is an important issue. Strategies to produce a secreted particle, either by manipulation of its composition or by co-expression of NS protein(s) will be also discussed, since this can lead to an easier purification process and to a decrease in product losses due to intracellular proteolysis. The production of Rotavirus-Hke particles and Bluetongue virus-like particles production will be used as examples to illustrate this point. 

Different approaches have been reported in the Hterature regarding the number of genes cloned in the same baculovirus. Pioneering work has been done at Prof Polly Roy s laboratory at Oxford University for Bluetongue virus (BTV) CLP and VLP production, where these authors generated BTV-CLP and BTV-VLP of different types and monomer compositions [4,13-16]. 

Bluetongue virus, the prototype virus of the Orbivirus genus in the Reoviridae family, is an non-enveloped virus with seven structural proteins (VP1-VP7) [12]. The outer capsid consists of two proteins, VP2 and VPS. The core exhibits icosahedral symmetry and is composed of five proteins, two major (VPS and VP7) and three minor (VP1,VP4 and VP6) classified according to... 

French TJ, Roy P (1990), Synthesis of bluetongue virus (BTV) core-like particles by a recombinant baculovirus expressing the two major structural core proteins of BTV, J. Virol. 64 1530-1536. 

Hyatt AD, Zhao Y, Roy P (1993), Release of bluetongue virus-like particles from insect cells is mediated by BTV nonstructural protein NS3/NS3A, Virology 193 592-603. 

Le Blois H, Fayard B, Urakawa T, Roy P (1991), Synthesis and characterization of chimeric particles between epizootic hemorrhagic disease virus and bluetongue virus functional domains are conserved on the VP3 protein, J. Virol. 65 4821-4831. 

Roy P (1990), Use of baculovirus expression vectors development of diagnostic reagents, vaccines and morphological counterparts of bluetongue virus, FEMS Microbiol. Immunol. 2 223-234. 

Fig. 5. Structural classification of Reoviridae architecture, (a) Bluetongue virus, a typical orbivirus (Grimes et al, 1998). (b) Orthoreovirus, a typical reovirus (Reinisch et al, 2000). (c) CPV, a typical cypovirus (Hill et ai, 1999).

Fig. 8. Illustration of helices and sheets at 7 A by a simulated density map. The atomic model of a VP7 monomer of bluetongue virus (Grimes et at, 1998) was obtained from the Protein Data Bank and rendered as ribbons (a). The same model was then Gaussian filtered to 7 A to generate a density map, which is displayed as shaded surfaces, from left to right, using gradually increasing contour levels (b). [Courtesy of Dr. Matthew L. Baker.]...

The first structure was of the bluetongue virus VP7 protein (Grimes et al, 1995), which has two domains. The central part of the sequence (residues 121-249) forms a (3 sandwich (or distorted barrel) most like... 

The fxS protein is associated with the fil protein, and a complex of these proteins has been determined (Liemann et al., 2002). /il forms a T=13 layer in the reovirus particles but is not present in the crystal structure of the capsid (Reinisch et al., 2000). The protein is similar to OrbivirusYPl in that it has a jelly-roll domain positioned external to a base formed mostly by helices. The jelly-roll domain contains a few extra strands, and in the sequence it is flanked by the residues forming the helical region. Although this is true also for the corresponding region in VP7 of bluetongue virus, the fold in this part of the protein is different. 

Taraporewala, Z., Chen, D., and Patton, J. (2001). Multimers of the bluetongue virus nonstructural protein, NS2, possess nucleotidyl phosphatase activity Similarities between NS2 and rotavirus NSP2. Virology 280, 221-231. 

Zhao, Y, Thomas, C., Bremer, C., and Roy, P. (1994). Deletion and mutational analyses of bluetongue virus NS2 protein indicate that the amino but not the carboxy terminus of the protein is critical for RNA-protein interactions. J. Virol. 68, 2179-2185. 

Bragg reflection/diffraction point, 40 Brome mosaic virus (BMV), 203 Bromoviridae, 152, 153 BTV. See Bluetongue virus (BTV)... 

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