Intracellular distribution of poliovirus proteins and the induction of virus-specific cytoplasmic structures

Bienz, Kurt; Egger, Denise; Rasser, Y.; Bossart, Walter

doi:10.1016/0042-6822(83)90531-7

Cited by 171 publications

(157 citation statements)

References 29 publications

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“…Previous reports have indicated that the PV protein 2BC is the inducing protein for PV vesicle formation (1,13,20) and that the PV nonstructural protein 3A may contribute to the final morphology (73). Thus, it was of interest to determine whether vesicle formation initiated by protein 2BC would also be mediated by the COPII mechanism.…”

Section: Vol 75 2001 Poliovirus Vesicles Are Copii Coated and Er Dementioning

confidence: 99%

“…They are exclusively associated with the membranes of the vesicles of the PV replication complex and can, therefore, be used as a histochemical marker for PV vesicles and the viral replication complex (10,11,24,67). Several reports indicate that protein 2BC, in the absence of or in combination with other viral proteins, can induce vesicle formation (1,13,20,73,79,80). The mechanism by which protein 2BC induces vesicles is not known, and thus it is not clear whether vesicle induction and formation are an intrinsic property of this viral protein or whether 2BC might interact with (i.e., activate or stimulate) cellular vesiculation processes.…”

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confidence: 99%

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Cellular COPII Proteins Are Involved in Production of the Vesicles That Form the Poliovirus Replication Complex

Rust¹,

Landmann²,

Gosert³

et al. 2001

J Virol

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202

207

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Poliovirus (PV) replicates its genome in association with membranous vesicles in the cytoplasm of infected cells. To elucidate the origin and mode of formation of PV vesicles, immunofluorescence labeling with antibodies against the viral vesicle marker proteins 2B and 2BC, as well as cellular markers of the endoplasmic reticulum (ER), anterograde transport vesicles, and the Golgi complex, was performed in BT7-H cells. Optical sections obtained by confocal laser scanning microscopy were subjected to a deconvolution process to enhance resolution and signal-to-noise ratio and to allow for a three-dimensional representation of labeled membrane structures. The mode of formation of the PV vesicles was, on morphological grounds, similar to the formation of anterograde membrane traffic vesicles in uninfected cells. ER-resident membrane markers were excluded from both types of vesicles, and the COPII components Sec13 and Sec31 were both found to be colocalized on the vesicular surface, indicating the presence of a functional COPII coat. PV vesicle formation during early time points of infection did not involve the Golgi complex. The expression of PV protein 2BC or the entire P2 and P3 genomic region led to the production of vesicles carrying a COPII coat and showing the same mode of formation as vesicles produced after PV infection. These results indicate that PV vesicles are formed at the ER by the cellular COPII budding mechanism and thus are homologous to the vesicles of the anterograde membrane transport pathway.Poliovirus (PV), the prototype member of the family Picornaviridae, contains an RNA genome of plus polarity with a single large open reading frame (ORF) coding for a polyprotein of 265 kDa. The translation product is cleaved by intrinsic viral proteases into about 20 proteins, of which intermediate as well as end products are functional (38, 83, 88; reviewed in reference 35). The proteins encoded by the P1 genomic region form the capsid, whereas most of the nonstructural proteins, encoded by the P2 and P3 genomic region, are involved in viral RNA replication (2,27,28,37,48,55,58,82). The viral genome replicates asymmetrically with an excess of plus strands produced in multistranded replicative intermediates (2,17,31,49). PV genome replication depends on the template RNA molecule carrying a cis-acting replicative element (see references 32 and 54), a primer (54), viral and cellular proteins and their proper interactions (2,29,30,53), and the presence of membranes (10,12,14,26,74).Genome replication of all plus-strand RNA viruses investigated so far takes place in membrane-bound replication complexes (see references 19 and 65 and references therein). However, the morphology of such replication complexes of different viruses is diverse, and different cellular compartments provide membranes for and are involved in viral replication (44,56,65). PV replication complexes are built up from individual membranous vesicles (PV vesicles) which are assembled into specific higher-order structures (11,12,15).The PV replicat...

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Section: Vol 75 2001 Poliovirus Vesicles Are Copii Coated and Er Dementioning

confidence: 99%

mentioning

confidence: 99%

Cellular COPII Proteins Are Involved in Production of the Vesicles That Form the Poliovirus Replication Complex

Rust¹,

Landmann²,

Gosert³

et al. 2001

J Virol

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202

207

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“…It is thought that the 2C protein attaches to vesicular membranes and is associated with viral RNA synthesis (Bienz et al, 1983;Takegami et al, 1983), although its exact function is obscure.…”

Section: Non-structural Proteinsmentioning

confidence: 99%

The Complete Nucleotide Sequence of Swine Vesicular Disease Virus

Inoue

Suzuki

Sekiguchi

1989

Journal of General Virology

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SUMMARYThe complete nucleotide sequence of the genome of the enterovirus swine vesicular disease virus (SVDV ; H/3 '76) isolated from a healthy pig has been determined using molecular cloning and DNA sequencing techniques. The RNA genome was 7400 nucleotides long, excluding the poly(A) tract, and appeared to encode a single polyprotein of 2185 amino acids. The predicted amino acid sequence of the polyprotein showed close homology (around 90 ~) to that of the previously sequenced coxsackieviruses B1, B3 and B4, and also showed homology (around 60~) to that of poliovirus. This homology allows us to predict the possible cleavage sites of the polyprotein and to identify other features of structural and functional significance, which seem to be important to the biological integrity of the virus. A detailed analysis of homology between SVDV and coxsackieviruses shows that non-structural proteins are highly conserved whereas the structural proteins are less well conserved. The 5' and 3' noncoding regions are also conserved, although there are several divergent nuclcotide stretches. These stretches may differentiate SVDV from coxsackieviruses.

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“…For example, mammalian cells infected with Kunjin virus, a flavivirus, display various membrane morphologies that have been termed convoluted membranes and vesicle packets, which contain markers from the intermediate compartment and the trans-Golgi network, respectively (52,53,77). Cells infected with poliovirus, a picornavirus, accumulate large numbers of membranous vesicles derived from the endoplasmic reticulum (ER) that range in diameter from 150 to 400 nm (6,7,13,27,(72)(73)(74)76) and that display characteristics similar to those of cellular autophagic vacuoles (18,68,72). Finally, cells infected with bovine viral diarrhea virus (BVDV), a pestivirus, contain tubules and spherical vesicles that are 100 to 200 nm in diameter and that are thought to be derived from the rough ER (33).…”

mentioning

confidence: 99%

Nonstructural Protein Precursor NS4A/B from Hepatitis C Virus Alters Function and Ultrastructure of Host Secretory Apparatus

Konan

Giddings

Ikeda

et al. 2003

J Virol

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Intracellular distribution of poliovirus proteins and the induction of virus-specific cytoplasmic structures

Cited by 171 publications

References 29 publications

Cellular COPII Proteins Are Involved in Production of the Vesicles That Form the Poliovirus Replication Complex

Cellular COPII Proteins Are Involved in Production of the Vesicles That Form the Poliovirus Replication Complex

The Complete Nucleotide Sequence of Swine Vesicular Disease Virus

Nonstructural Protein Precursor NS4A/B from Hepatitis C Virus Alters Function and Ultrastructure of Host Secretory Apparatus

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