Reproduction of Rhabdoviruses

Wagner, Robert R.

doi:10.1007/978-1-4684-2706-6_1

Cited by 176 publications

(147 citation statements)

References 261 publications

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“…about 18o000 to 2ooooo), are found associated with purified virus nucleocapsids (Obijeski et al ~976a). The function of L protein is not yet known, but a large protein found associated with rhabdoviruses is believed to be a virion-associated transcriptase component (Wagner, 1975). Recently a large protein (mol.…”

Section: Review: Bunyaviruses 5 Chemical Composition Proteins Of Virumentioning

confidence: 99%

Bunyaviridae: Recent Biochemical Developments

Obijeski

Murphy

1977

Journal of General Virology

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Section: Review: Bunyaviruses 5 Chemical Composition Proteins Of Virumentioning

confidence: 99%

Bunyaviridae: Recent Biochemical Developments

Obijeski

Murphy

1977

Journal of General Virology

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“…Negative-strand RNA viruses encapsidate their genome in ribonucleoprotein particles (RNP) (Baltimore, 1971 ;Wagner, 1975) which can support viral transcription and replication. In vesicular stomatitis virus (VSV), these particles contain three of the five VSV proteins: the polymerase (L), the nucleocapsid protein (N) and the phosphoprotein (NS).…”

Section: Introductionmentioning

confidence: 99%

Cloning and Expression of a Viral Phosphoprotein: Structure Suggests Vesicular Stomatitis Virus NS May Function by Mimicking an RNA Template

Hudson¹,

Condra²,

Lazzarini³

1986

Journal of General Virology

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SUMMARYThe phosphoprotein (NS) gene from the Indiana serotype of vesicular stomatitis virus (VSV; Mudd-Summers strain) was cloned and sequenced. The NS gene encodes a protein of 265 amino acids which was expressed from a simian virus 40 vector in COS cells. The post-translational modification characteristic of viral NS, the extensive phosphorylation of a cluster of serine and threonine residues, was also evident in recombinant NS protein. The NS gene displays a property common to the phosphoprotein genes of negative-strand RNA viruses: the phosphoprotein mRNA has a second open reading frame (ORF) which could encode a small (7500 mol. wt.) protein. Both measles virus and Sendai virus employ the second ORF of their phosphoprotein gene, and the resultant proteins have an amino acid composition similar to that predicted for the VSV ORF. Comparison of phosphoproteins from different VSV strains revealed two conserved domains that we propose are critical for the function of NS in transcription and replication.

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“…In contrast to the differential effects of monensin on VSV and influenza virus replication previously observed in monolayer cultures of MDCK cells, yields of both viruses were found to be significantly reduced by high concentrations of monensin in suspension cultures, indicating that cellular architecture may play a role in determining the sensitivity of virus replication to the drug. Nigericin, an ionophore that facilitates transport of potassium ions across membranes, blocked the replication of both influenza virus and VSV in MDCK cell monolayers, indicating that the ion specificity of ionophores influences their effect on the replication of enveloped viruses.Cells infected with enveloped RNA viruses provide valuable systems for elucidating the pathways involved in subcellular transport of membrane glycoproteins (8,20,44). As a result of viral inhibition of host protein synthesis, only one or a few viral membrane glycoproteins are synthesized in infected cells.…”

mentioning

confidence: 99%

“…Cells infected with enveloped RNA viruses provide valuable systems for elucidating the pathways involved in subcellular transport of membrane glycoproteins (8,20,44). As a result of viral inhibition of host protein synthesis, only one or a few viral membrane glycoproteins are synthesized in infected cells.…”

mentioning

confidence: 99%

Modulation of glycosylation and transport of viral membrane glycoproteins by a sodium ionophore.

Alonso-Caplen¹,

Compans²

1983

The Journal of Cell Biology

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Analysis of viral glycoprotein expression on surfaces of monensin-treated cells using a fluorescence-activated cell sorter (FACS) demonstrated that the sodium ionophore completely inhibited the appearance of the vesicular stomatitis virus (VSV) G protein on (Madin-Darby canine kidney) MDCK cell surfaces. In contrast, the expression of the influenza virus hemagglutinin (HA) glycoprotein on the surfaces of MDCK cells was observed to occur at high levels, and the time course of its appearance was not altered by the ionophore. Viral protein synthesis was not inhibited by monensin in either VSV-or influenza virus-infected cells. However, the electrophoretic mobilities of viral glycoproteins were altered, and analysis of pronase-derived glycopeptides by gel filtration indicated that the addition of sialic acid residues to the VSV G protein was impaired in monensin-treated cells. Reduced incorporation of fucose and galactose into influenza virus HA was observed in the presence of the ionophore, but the incompletely processed HA protein was cleaved, transported to the cell surface, and incorporated into budding virus particles. In contrast to the differential effects of monensin on VSV and influenza virus replication previously observed in monolayer cultures of MDCK cells, yields of both viruses were found to be significantly reduced by high concentrations of monensin in suspension cultures, indicating that cellular architecture may play a role in determining the sensitivity of virus replication to the drug. Nigericin, an ionophore that facilitates transport of potassium ions across membranes, blocked the replication of both influenza virus and VSV in MDCK cell monolayers, indicating that the ion specificity of ionophores influences their effect on the replication of enveloped viruses.Cells infected with enveloped RNA viruses provide valuable systems for elucidating the pathways involved in subcellular transport of membrane glycoproteins (8,20,44). As a result of viral inhibition of host protein synthesis, only one or a few viral membrane glycoproteins are synthesized in infected cells. These viruses possess limited genetic capacity, and the glycosylation and transport of their membrane glycoproteins to the cell surface are probably carried out by the same systems used by the host cell for biogenesis of its own membrane glycoproteins.Monovalent ionophores such as monensin, which is reported to interfere with the translocation of secretory as well as most membrane glycoproteins, have been used to characterize the pathways of intracellular glycoprotein transport in eucaryotic cells (18,(37)(38)(39)(40)(41)43). In addition, the effects of monensin on IgM and H2 glycosylation in lymphoid cells and fibronectin glycosylation in cultured human fibroblasts, as well as its influence on oligosaccharide maturation of

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Reproduction of Rhabdoviruses

Cited by 176 publications

References 261 publications

Bunyaviridae: Recent Biochemical Developments

Bunyaviridae: Recent Biochemical Developments

Cloning and Expression of a Viral Phosphoprotein: Structure Suggests Vesicular Stomatitis Virus NS May Function by Mimicking an RNA Template

Modulation of glycosylation and transport of viral membrane glycoproteins by a sodium ionophore.

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