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Open AccessJournal ArticleDOI

Intracellular Distribution of Rubella Virus Nonstructural Protein P150

TLDR
Antiserum prepared against an amino-terminal fragment of rubella virus (RUB) nonstructural polyprotein was used to study RUB-infected Vero cells, indicating that these structures may be the sites of viral RNA synthesis.
Abstract
Antiserum prepared against an amino-terminal fragment of rubella virus (RUB) nonstructural polyprotein was used to study RUB-infected Vero cells. Replicase protein P150 was associated with vesicles and vacuoles of endolysosomal origin and later with large, convoluted, tubular membrane structures. Newly incorporated bromouridine was associated with the same structures and specifically with small membrane invaginations, spherules, indicating that these structures may be the sites of viral RNA synthesis.

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Citations
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Journal ArticleDOI

Modification of intracellular membrane structures for virus replication

TL;DR: How viruses modify intracellular membranes is described, similarities between the structures that are induced by viruses of different families are highlighted and how these structures could be formed are discussed.
Journal ArticleDOI

A Positive-Strand RNA Virus Replication Complex Parallels Form and Function of Retrovirus Capsids

TL;DR: It is shown that brome mosaic virus RNA replication protein 1a, 2a polymerase, and a cis-acting replication signal recapitulate the functions of Gag, Pol, and RNA packaging signals in conventional retrovirus and foamy virus cores, revealing fundamental similarities in replication and may have common evolutionary origins.
Book ChapterDOI

Viral RNA replication in association with cellular membranes.

TL;DR: All plus-strand RNA viruses replicate in association with cytoplasmic membranes of infected cells, and studies of individual nonstructural proteins have revealed that the replication complexes are associated with the membranes and targeted to the respective organelle by the ns proteins rather than RNA.
Journal ArticleDOI

The endoplasmic reticulum provides the membrane platform for biogenesis of the flavivirus replication complex.

TL;DR: It is shown that the virus-induced recruitment of host proteins and membrane appears to occur at a pre-Golgi step and that a majority of the viral RNA species housed within the RC is in a double-stranded RNA (dsRNA) form.
Journal ArticleDOI

Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle.

TL;DR: The results identify spherules as the site of protein A and nascent RNA accumulation and define spherule topology, dimensions, and stoichiometry to reveal the nature and many details of the organization and function of the FHV RNA replication complex.
References
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Journal ArticleDOI

The alphaviruses: gene expression, replication, and evolution.

TL;DR: This article corrects the article on p. 496 in vol.
Journal Article

A new method of preparing gold probes for multiple-labeling cytochemistry

TL;DR: The usefulness of the new gold probes bound to protein A for multiple labeling in a current immunocytochemical study on receptor mediated transport of IgA in human duodenal crypt cells is demonstrated.
Journal ArticleDOI

Evolution and Taxonomy of Positive-Strand RNA Viruses: Implications of Comparative Analysis of Amino Acid Sequences

TL;DR: It is hypothesized that all positive-strand RNA viruses and some related double-stranded RNA viruses could have evolved from a common ancestor virus that contained genes for RNA-dependent RNA polymerase, a chymotrypsin-related protease that also functioned as the capsid protein, and possibly an RNA helicase.
Journal ArticleDOI

Membrane transport in the endocytic pathway

TL;DR: Despite controversies and debates, some fundamental properties of endosomes become apparent when comparing results from in vivo and in vitro strategies used to study endosomal membrane traffic.
Journal ArticleDOI

Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes.

TL;DR: It is shown that the RNA replicase of Semliki Forest and Sindbis virus is located in complex ribonucleoprotein structures associated with the cytoplasmic surface of modified secondary lysosomes and endosomes.
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