Characterization of Nodamura virus, an arthropod transmissible picornavirus

Murphy, Frederick A.; Scherer, William F.; Harrison, Alyne K.; Dunne, H. W.; Gary, G. William

doi:10.1016/0042-6822(70)90147-9

Cited by 46 publications

(26 citation statements)

References 17 publications

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“…4I). These aggregates most probably represented progeny virus particles that are known to form large paracrystalline arrays at late stages of infection (14,26,33). Note that the coat protein antibody used in these experiments does not distinguish between unassembled and assembled protein subunits.…”

Section: Vol 83 2009mentioning

confidence: 99%

Dual Roles for an Arginine-Rich Motif in Specific Genome Recognition and Localization of Viral Coat Protein to RNA Replication Sites in Flock House Virus-Infected Cells

Venter

Marshall

Schneemann

2009

J Virol

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Assembly of many RNA viruses entails the encapsidation of multiple genome segments into a single virion, and underlying mechanisms for this process are still poorly understood. In the case of the nodavirus Flock House virus (FHV), a bipartite positive-strand RNA genome consisting of RNA1 and RNA2 is copackaged into progeny virions. In this study, we investigated whether the specific packaging of FHV RNA is dependent on an arginine-rich motif (ARM) located in the N terminus of the coat protein. Our results demonstrate that the replacement of all arginine residues within this motif with alanines rendered the resultant coat protein unable to package RNA1, suggesting that the ARM represents an important determinant for the encapsidation of this genome segment. In contrast, replacement of all arginines with lysines had no effect on RNA1 packaging. Interestingly, confocal microscopic analysis demonstrated that the RNA1 packaging-deficient mutant did not localize to mitochondrial sites of FHV RNA replication as efficiently as wild-type coat protein. In addition, gain-of-function analyses showed that the ARM by itself was sufficient to target green fluorescent protein to RNA replication sites. These data suggest that the packaging of RNA1 is dependent on trafficking of coat protein to mitochondria, the presumed site of FHV assembly, and that this trafficking requires a high density of positive charge in the N terminus. Our results are compatible with a model in which recognition of RNA1 and RNA2 for encapsidation occurs sequentially and in distinct cellular microenvironments.

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Section: Vol 83 2009mentioning

confidence: 99%

Dual Roles for an Arginine-Rich Motif in Specific Genome Recognition and Localization of Viral Coat Protein to RNA Replication Sites in Flock House Virus-Infected Cells

Venter

Marshall

Schneemann

2009

J Virol

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“…Antibodies against N o d a m u r a virus have been detected in swine and some birds without clinical symptoms [33]. When inoculated into suckling mice or hamsters, NV produces flaccid paralysis and death of these vertebrate hosts [16,25,33]. NV can also replicate in hamster (BHK-21) or mosquito (Aedes albopictus) cell cultures without apparent cytopathic effect [i].…”

Section: Introductionmentioning

confidence: 99%

“…Both singlestranded messenger RNA molecules, RNA 1 and RNA 2, with respectively 1 and 0.5 × 10 6 daltons of molecular weight are encapsidated in a single virion [25,26]. RNA 1 serves as messenger for protein A, a putative replicase, while the coat protein precursor is translated by RNA 2 [27].…”

Section: Introductionmentioning

confidence: 99%

Implication of mitochondria in the replication of Nodamura virus in larvae of the Lepidoptera,Galleria mellonella (L.) and in suckling mice

Garzón

Strykowski

Charpentier

1990

Archives of Virology

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The replication of Nodamura virus, type species of the family Nodaviridae, takes place principally into the interfibrillar spaces of the sarcoplasm in close association with mitochondria in the infected muscles of both G. mellonella and suckling mice. The most striking event in infection of G. mellonella muscle cells was the aggregation and shape modification of numerous mitochondria (elongation, interdigitation, and vesiculation) at an early stage of infection. These clusters of mitochondria were cemented by a thick electron-dense material at the periphery of which viral particles undergo maturation process. In a later stage, degenerated and dilated mitochondria showed a clear assembling of virus particles on their outer membrane and occasionally on some inner membranes. These facts and the localization of RNA by RNase-gold technique in the assembling sites of viruses around and inside the mitochondria allowed us to postulate a role for the mitochondria as supports and/or energy suppliers for viral RNA synthesis and translation.

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“…The virus replicated in various insects, mosquito and BHK cell cultures and also caused mortality in suckling mice (Bailey & Scott, 1973;Bailey et al, 1975;Tesh, 1980). While initial information pointed to the virus being an arbovirus, or even a picornavirus, on the basis of its physicochemical properties (Murphy et al, 1970) the demonstration by Newman & Brown (1973) that mouse-grown virus contained two pieces of RNA pointed to this virus being a novel type. The two RNA species have mol.…”

Section: The Nodamura Virus Family General Characteristicsmentioning

confidence: 99%

General Characteristics, Gene Organization and Expression of Small RNA Viruses of Insects

Moore

Reavy

King

1985

Journal of General Virology

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Characterization of Nodamura virus, an arthropod transmissible picornavirus

Cited by 46 publications

References 17 publications

Dual Roles for an Arginine-Rich Motif in Specific Genome Recognition and Localization of Viral Coat Protein to RNA Replication Sites in Flock House Virus-Infected Cells

Dual Roles for an Arginine-Rich Motif in Specific Genome Recognition and Localization of Viral Coat Protein to RNA Replication Sites in Flock House Virus-Infected Cells

Implication of mitochondria in the replication of Nodamura virus in larvae of the Lepidoptera,Galleria mellonella (L.) and in suckling mice

General Characteristics, Gene Organization and Expression of Small RNA Viruses of Insects

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