PubMed HealthSearch

PubMed · 2989864

Speciation in orbiviruses.

Abstract

The definition of Orbivirus species should be based on the ability of virus populations to reassort genetic information. Application of the definition of biological species to orbiviruses enables consideration to be given the evolutionary tendencies of virus populations and to mechanisms for generating diversity within orbiviruses.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

B M Gorman. 1985. Speciation in orbiviruses.. https://pubmed.ncbi.nlm.nih.gov/2989864/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Preliminary crystallographic study of bluetongue virus capsid protein, VP7.

Bluetongue virus serotype 10 (BTV-10) VP7, expressed by insect cells infected with the recombinant baculovirus, has been purified and crystallized. Two crystal forms suitable for X-ray analysis have been obtained. Type I crystals belong to space group P6(3)22 with a = b = 95.2 A, c = 181.0 A, alpha = beta = 90 degrees gamma = 120.0 degrees, and contain a single subunit in the crystallographic asymmetric unit. They diffract to dmin = 3.0 A. Type II crystals belong to space group P2(1) with a = 69.4 A, b = 97.1 A, c = 71.4 A, beta = 109.0 degrees, and contain a trimer in the crystallographic asymmetric unit. They diffract to dmin = 2.1 A. These results, together with solution studies, show that the molecule is a trimer.

Bluetongue virus

Interaction of nucleic acids with core-like and subcore-like particles of bluetongue virus.

Bluetongue virus (BTV) core-like particles (CLPs) were synthesized by coexpression of VP3 and VP7 using a dual recombinant baculovirus. Purified CLPs were shown to bind single-stranded RNA in three different assay systems: gel retardation, nitrocellulose binding, and sucrose gradient sedimentation. CLPs showed equal affinity for BTV-specific and non-BTV RNA and also bound DNA. RNAase protection experiments demonstrated that bound RNA was accessible to immobilized ribonuclease, suggesting that the RNA was predominantly present on the outside of the CLPs. By using individually purified VP7 and VP3 in separate assays, the binding activity was shown to reside on VP3. These results indicate further functional homologies between BTV VP3 and the rotavirus inner-core VP2 protein.

Bluetongue virus

The expressed VP4 protein of bluetongue virus binds GTP and is the candidate guanylyl transferase of the virus.

A minor core protein, VP4, of bluetongue virus serotype 10 (BTV-10) has been synthesized in insect cells infected with a genetically manipulated recombinant baculovirus. When insect cells were coinfected by this recombinant virus and a recombinant baculovirus expressing the two major core proteins (VP3 and VP7) of the virus, core-like particles (CLPs) consisting of all three proteins were formed. Purified CLPs reacted with [32P]GTP which was covalently bound to VP4 only. Similarly reconstituted CLPs with VP1 or VP6 did not form covalent complexes with [32P]GTP. The virion-derived VP4 was also shown to have GTP-binding activity. The covalent binding of GTP indicates that expressed VP4 not only is biologically active but also is the candidate guanylyl transferase of the virus. The optimum reaction conditions for GTP binding by VP4 have been investigated.

Bluetongue virus