» Articles » PMID: 2154600

Structural Organization of Poliovirus RNA Replication is Mediated by Viral Proteins of the P2 Genomic Region

Overview
Journal J Virol
Date 1990 Mar 1
PMID 2154600
Citations 121
Authors
Affiliations
Soon will be listed here.
Abstract

Transcriptionally active replication complexes bound to smooth membrane vesicles were isolated from poliovirus-infected cells. In electron microscopic, negatively stained preparations, the replication complex appeared as an irregularly shaped, oblong structure attached to several virus-induced vesicles of a rosettelike arrangement. Electron microscopic immunocytochemistry of such preparations demonstrated that the poliovirus replication complex contains the proteins coded by the P2 genomic region (P2 proteins) in a membrane-associated form. In addition, the P2 proteins are also associated with viral RNA, and they can be cross-linked to viral RNA by UV irradiation. Guanidine hydrochloride prevented the P2 proteins from becoming membrane bound but did not change their association with viral RNA. The findings allow the conclusion that the protein 2C or 2C-containing precursor(s) is responsible for the attachment of the viral RNA to the vesicular membrane and for the spatial organization of the replication complex necessary for its proper functioning in viral transcription. A model for the structure of the viral replication complex and for the function of the 2C-containing P2 protein(s) and the vesicular membranes is proposed.

Citing Articles

Antiviral Development for the Polio Endgame: Current Progress and Future Directions.

Xie H, Rhoden E, Liu H, Ogunsemowo F, Mainou B, Burke R Pathogens. 2024; 13(11).

PMID: 39599522 PMC: 11597170. DOI: 10.3390/pathogens13110969.


Enzymatic characterization and dominant sites of foot-and-mouth disease virus 2C protein.

Zhou S, Liu N, Tian Y, Pan H, Han Y, Li Z Heliyon. 2024; 10(15):e35449.

PMID: 39170175 PMC: 11336754. DOI: 10.1016/j.heliyon.2024.e35449.


Enteroviral 2C protein is an RNA-stimulated ATPase and uses a two-step mechanism for binding to RNA and ATP.

Yeager C, Carter G, Gohara D, Yennawar N, Enemark E, Arnold J Nucleic Acids Res. 2022; 50(20):11775-11798.

PMID: 36399514 PMC: 9723501. DOI: 10.1093/nar/gkac1054.


The introduction of mutations in the wild type coxsackievirus B3 (CVB3) IRES RNA leads to different levels of in vitro reduced replicative and translation efficiencies.

Gharbi J, Almalki M, Mhadheb M PLoS One. 2022; 17(10):e0274162.

PMID: 36190999 PMC: 9529112. DOI: 10.1371/journal.pone.0274162.


Involvement of a Nonstructural Protein in Poliovirus Capsid Assembly.

Adeyemi O, Sherry L, Ward J, Pierce D, Herod M, Rowlands D J Virol. 2018; 93(5).

PMID: 30541849 PMC: 6384072. DOI: 10.1128/JVI.01447-18.


References
1.
CALIGUIRI L, Tamm I . Action of guanidine on the replication of poliovirus RNA. Virology. 1968; 35(3):408-17. DOI: 10.1016/0042-6822(68)90219-5. View

2.
Butterworth B, Shimshick E, Yin F . Association of the polioviral RNA polymerase complex with phospholipid membranes. J Virol. 1976; 19(2):457-66. PMC: 354883. DOI: 10.1128/JVI.19.2.457-466.1976. View

3.
CALIGUIRI L, Tamm I . Membranous structures associated with translation and transcription of poliovirus RNA. Science. 1969; 166(3907):885-6. DOI: 10.1126/science.166.3907.885. View

4.
Noble J, LEVINTOW L . Dynamics of poliovirus-specific RNA synthesis and the effects of inhibitors of virus replication. Virology. 1970; 40(3):634-42. DOI: 10.1016/0042-6822(70)90208-4. View

5.
Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View