Poliovirus Assembly and Encapsidation of Genomic RNA

Ansardi, David C.; Porter, Donna C.; Anderson, Marie J.; Morrow, Casey D.

doi:10.1016/s0065-3527(08)60069-x

Cited by 35 publications

(12 citation statements)

References 219 publications

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“…In addition to the structural proteins and precursors, some nonstructural proteins including proteins 2C, 3D, 2A, and 3CD were also detected in DIMs. The presence of low levels of proteases 2A and 3CD is consistent with their respective roles in the cleavage of P1 from the polyprotein precursor and the subsequent hydrolysis of P1 into VP0, VP3, and VP1 (12). Both 2C and the poliovirus RNA polymerase 3D are essential for viral replication (12), and its presence in DIMs suggests that these membranes might be related to the membranous structures containing RNA replication complexes.…”

Section: A Specific Subset Of Poliovirus Proteins Are Present Inmentioning

confidence: 53%

“…Translation of the genomic RNA generates a 247 000 Da polyprotein that is cotranslationally processed into three precursors (P1, P2, and P3). P1 is the precursor of capsid proteins, whereas P2 and P3 proteolysis originates nonstructural proteins involved in vegetative viral functions (12). P1 is released from the polyprotein by the autocatalytic activity of viral proteinase 2A.…”

mentioning

confidence: 99%

“…To produce mature viral particles, five protomers give rise to a 14S pentamer and 12 of these pentamers assemble to form a provirion while incorporating the genomic RNA. During maturation of the virion, VP0 is cleaved to form capsid proteins VP4 and VP2 (12). The NH 2 -terminal glycine from capsid protein VP4 as well as of its precursors, VP0 and P1, is covalently modified by myristic acid (13,14).…”

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confidence: 99%

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The Amino-Terminal Nine Amino Acid Sequence of Poliovirus Capsid VP4 Protein Is Sufficient To Confer N-Myristoylation and Targeting to Detergent-Insoluble Membranes

Martı́n-Belmonte¹,

López-Guerrero²,

Carrasco³

et al. 2000

Biochemistry

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The confinement of membrane proteins by lipid-lipid interactions into specialized detergent-insoluble membrane (DIM) microdomains has been proposed as a general mechanism to recruit selectively lipid-modified proteins and specific transmembrane proteins. Poliovirus capsid VP4 protein and its precursors are myristoylated at the NH(2)-terminal Gly residue. To determine whether poliovirus uses DIMs during its replicative cycle, we isolated DIMs from poliovirus-infected HeLa cells and identified the presence of capsid proteins and their precursors, proteinases 2A and 3C, and other viral proteins involved in poliovirus RNA replication such as protein 2C and the polymerase 3D. The morphology of these DIMs was similar to that of the previously described rosette-like vesicles associated with replication complexes isolated from poliovirus-infected cells. To examine the possible role of the myristoyl moiety in the targeting of poliovirus structural proteins to DIMs, we generated a chimeric protein consisting of the nine amino-terminal amino acids from VP4 fused to the amino terminus of the green fluorescent protein (GFP). The selected VP4 sequence was sufficient to confer N-myristoylation and targeting to DIMs to the GFP chimera. Mutations within this sequence known to affect both myristoylation and poliovirus assembly abrogated the targeting of the GFP chimera. These results indicate that the myristoylated amino-terminal nonapeptide from poliovirus VP4 protein constitutes a signal for incorporation into DIMs.

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Section: A Specific Subset Of Poliovirus Proteins Are Present Inmentioning

confidence: 53%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The Amino-Terminal Nine Amino Acid Sequence of Poliovirus Capsid VP4 Protein Is Sufficient To Confer N-Myristoylation and Targeting to Detergent-Insoluble Membranes

Martı́n-Belmonte¹,

López-Guerrero²,

Carrasco³

et al. 2000

Biochemistry

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“…Viral replication starts with the synthesis of the minus strand, generating the double-stranded RNA, that is the replicative form, which subsequently becomes Review Article a replicative intermediate when many viral genomes are replicated simultaneously. The capsid proteins associate in protomers, five protomers form a pentamer and 12 pentamers form a procapsid [95]. It is not yet known whether the viral genome enters a preformed procapsid, or if in fact the capsid proteins condense around the viral genome to give the provirion.…”

Section: The Poliovirusmentioning

confidence: 99%

Molecular mechanisms of poliovirus persistence: key role of capsid determinants during the establishment phase

Pelletier

Duncan

Pavio

et al. 1998

Cellular and Molecular Life Sciences (CMLS)

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As viral persistence is of major medical importance, well-characterized, simple models are needed to improve our understanding of persistent infections. We have chosen to study the molecular mechanisms of viral persistence with the poliovirus (PV), because this picornavirus is one of the best characterized animal viruses, it infects the central nervous system which is a target organ for viral persistence, and it belongs to the Picornaviridae family of viruses, which includes several naturally persisting viruses. We have developed models of PV persistence in neuronal and epidermoid cells, and the present review will focus on the latter one because both lytic and persistent PV strains can be used to study the PV-HEp-2 cell interactions. The viral determinants of persistence have been investigated with this model, and PV determinants have proven to be of crucial importance for the establishment of persistence in HEp-2 cells. Precise determinants of PV persistence have been identified for PV serotypes 1 and 3, in capsid proteins VP1 and VP2. These determinants modify the early steps of the PV cycle, and in particular, the conformational modifications of the capsid following virus adsorption onto its receptor. These results permit us to propose several hypotheses concerning PV persistence and the early steps of the PV cycle.

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“…

The three serotypes of poliovirus (PV) belong to the Picornaviridae family [1,2] and they are small, non-enveloped viruses with a single-strand and positive polarity RNA genome [1,3] . Only 1-2% of the patients infected with any of the three serotypes of PV have paralytic poliomyelitis, mainly in the lower limbs caused by the destruction of motor neurons present in the central nervous system (CNS) [2,4] .

PV infection occurs through the oral route and the virus infects the digestive tract, especially the lymphatic tissue present in Peyer's patches and tonsils.

…”

mentioning

confidence: 99%

In vitro Interaction of Poliovirus with Cytoplasmic Dynein

2007

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Objective: Poliovirus (PV) enters the host by the oral route and can infect the central nervous system (CNS) by two mechanisms: crossing the blood-brain barrier and traveling along the nerves from the muscle to the spinal cord. In the latter mechanism, the PV receptor, CD155, and the motor protein, dynein, have been implicated in the transport of PV to the CNS. In this work we analyzed the possible interaction of PV with dynein. Methods: PV was bound to a Sepharose 4B beads and they were used to analyze the interaction of PV with cytoplasmic proteins from neuroblastoma cells by affinity chromatography and Western blot. Results: The interaction with cytoplasmic dynein was observed only when the Sepharose beads bound to PV were used and not in the control ones, where proteins from uninfected cells were coupled. Conclusion: These preliminary results open the possibility that PV uses the dynein directly in its retrograde axonal transport.

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Poliovirus Assembly and Encapsidation of Genomic RNA

Cited by 35 publications

References 219 publications

The Amino-Terminal Nine Amino Acid Sequence of Poliovirus Capsid VP4 Protein Is Sufficient To Confer N-Myristoylation and Targeting to Detergent-Insoluble Membranes

The Amino-Terminal Nine Amino Acid Sequence of Poliovirus Capsid VP4 Protein Is Sufficient To Confer N-Myristoylation and Targeting to Detergent-Insoluble Membranes

Molecular mechanisms of poliovirus persistence: key role of capsid determinants during the establishment phase

In vitro Interaction of Poliovirus with Cytoplasmic Dynein

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