Sequence and analysis of the capsid protein of Nudaurelia capensis ω virus, an insect virus with T = 4 icosahedral symmetry

Agrawal, Deepak K.; Johnson, John E.

doi:10.1016/0042-6822(92)90918-f

Cited by 45 publications

(39 citation statements)

References 18 publications

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“…The virus particles assemble as procapsids composed of 240 identical subunits that undergo maturation via assembly dependent autoproteolytic cleavage of the capsid protein precursor at its C terminus, leading to the production of the b and c peptides (Agrawal & Johnson, 1992;Hanzlik et al, 1995;Gordon et al, 1999). This cleavage of the capsid protein precursor results in stabilization of the virus particle, which is proposed to be important for infectivity (Munshi et al, 1996;Helgstrand et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Genome organization and translation products of Providence virus: insight into a unique tetravirus

Walter

Pringle

Nakayinga

et al. 2010

Journal of General Virology

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Providence virus (PrV) is a member of the family Tetraviridae, a family of small, positive-sense, ssRNA viruses that exclusively infect lepidopteran insects. PrV is the only known tetravirus that replicates in tissue culture. We have analysed the genome and characterized the viral translation products, showing that PrV has a monopartite genome encoding three ORFs: (i) p130, unique to PrV and of unknown function; (ii) p104, which contains a read-through stop signal, producing an N-terminal product of 40 kDa (p40) and (iii) the capsid protein precursor (p81). There are three 2A-like processing sequences: one at the N terminus of p130 (PrV-2A 1 ) and two more (PrV-2A 2 and PrV-2A 3 ) at the N terminus of p81. Metabolic radiolabelling identified viral translation products corresponding to all three ORFs in persistently infected cells and showed that the readthrough stop in p104 and PrV-2A 3 in p81 are functional in vivo and these results were confirmed by in vitro translation experiments. The RNA-dependent RNA polymerase domain of the PrV replicase is phylogenetically most closely related to members of the families Tombusviridae and Umbraviridae rather than to members of the family Tetraviridae. The unique genome organization, translational control systems and phylogenetic relationship with the replicases of (+ve) plant viruses lead us to propose that PrV represents a novel family of small insect RNA viruses, distinct from current members of the family Tetraviridae.

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Section: Introductionmentioning

confidence: 99%

Genome organization and translation products of Providence virus: insight into a unique tetravirus

Walter

Pringle

Nakayinga

et al. 2010

Journal of General Virology

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“…The capsid structure of NO)V was also shown to have T = 4 symmetry (Cavaretli et at., 1991). Sequencing the smaller 2-5 kb RNA of NoV demonstrated the potential to encode the coat proteins' precursor that is cleaved at a Asn-Phe site 74 residues from its C terminus (Agrawal & Johnson, 1992). Predicted amino acid sequences at the N terminus of the 8K protein (FAAAVLAFAANMLTSV) and an internal fragment of the 63K protein (PTLVDNGFWIGGNYALTPTS) are 88% and 94% identical, respectively, to the HaSV sequences we report.…”

Section: Presence O F Another F O R M O F H a S Vmentioning

confidence: 75%

“…The type member, NflV, has a monopartite genome of approximately 5 kb encased in a 38 nm capsid (density in CsC1 is 1.3 g/ml; Moore, 1991a) which was originally reported to be composed of a single major protein constituent of 60K. However, recent work has shown the presence in the capsid of a small protein of Mr approximately 8K (Agrawal & Johnson, 1992). …”

Section: Presence O F Another F O R M O F H a S Vmentioning

confidence: 99%

“…An anomalous provisional member of the Tetraviridae is NO)V. This virus shows a particularly close relationship to HaSV and was reported recently as having a 40 nm capsid composed of two 62K and 8K protein constituents and also a bipartite genome with ssRNA strands of approximately 5 kb and 2.5 kb (Agrawal & Johnson, 1992;Moore, 1991 a). The capsid structure of NO)V was also shown to have T = 4 symmetry (Cavaretli et at., 1991).…”

Section: Presence O F Another F O R M O F H a S Vmentioning

confidence: 99%

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A novel small RNA virus isolated from the cotton bollworm, Helicoverpa armigera

Hanzlik

Dorrian

Gordon

et al. 1993

Journal of General Virology

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A small RNA virus with novel characteristics has been isolated from laboratory-bred larvae of Helicoverpa armigera. Infection by the H. armigera stunt virus causes severe retardation of larval development and subsequent death. Its particles are isometric, 38 nm in diameter, and have a buoyant density of 1.296 g/ml in caesium chloride.The viral capsid has two major non-glycosylated protein components with Mrs of 65 000 and 6000, and contains

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“…A member of the family Tetraviridae, NwV is a bipartite virus with two messenger-sense RNA's (Agrawal & Johnson, 1992). Each of the 240 subunits contains 645 amino acids and the subunits assemble into a provirion.…”

Section: Introductionmentioning

confidence: 99%

Production and crystallization of virus-like particles assembled in a heterologous protein expression system

McKinney¹,

Agrawal²,

Fisher³

et al. 1994

Acta Cryst D

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It is of considerable interest to separate the processes of viral infectivity and virion assembly. Until recently this has only been possible with viruses that could be disassembled and reassembled in vitro. Even in these cases it was difficult to establish the authenticity of reassembled capsid protein because of possible irreversible damage that may have occurred to the protein during disassembly. An ideal method for the study of virus assembly is a protein expression system in which conditions are appropriate for spontaneous particle formation from freshly synthesized polypeptides. The baculovirus expression system has proven to be an excellent means to this end. Recently, this approach has been used to study the T = 3 Flock House insect virus and it has been demonstrated that subunits with the wild-type protein sequence, and with site-specific mutations that prevent particle maturation, will assemble and crystallize. This same approach has now been used at Purdue to study the T = 4 Nudaurelia to capensis insect virus. There is no cell culture system currently available for the study of NtoV, thus the expression system provides the first opportunity to study assembly under controlled conditions. Abbreviations ADA, N-(a-acetamido)-2-iminodiacetic acid, N-(carbamoylmethyl)iminodiacetic acid (from Sigma Chemicals). BME, /3-mercaptoethanol. HEPES, N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid.

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Sequence and analysis of the capsid protein of Nudaurelia capensis ω virus, an insect virus with T = 4 icosahedral symmetry

Cited by 45 publications

References 18 publications

Genome organization and translation products of Providence virus: insight into a unique tetravirus

Genome organization and translation products of Providence virus: insight into a unique tetravirus

A novel small RNA virus isolated from the cotton bollworm, Helicoverpa armigera

Production and crystallization of virus-like particles assembled in a heterologous protein expression system

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