Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; Picornavirales; Picornaviridae; Enterovirus.
Polypyrimidine tract-binding protein stimulates the poliovirus IRES by modulating eIF4G binding
An RNA element at the 5'-end of the poliovirus genome functions as a general promoter for RNA synthesis
Replication of poliovirus requires binding of the poly(rC) binding protein to the cloverleaf as well as to the adjacent C-rich spacer sequence between the cloverleaf and the internal ribosomal entry site
Interaction of translation initiation factor eIF4B with the poliovirus internal ribosome entry site
Poly (rC) binding protein 2 forms a ternary complex with the 5'-terminal sequences of poliovirus RNA and the viral 3CD proteinase
Cis-element, oriR, involved in the initiation of (-) strand poliovirus RNA: a quasi-globular multi-domain RNA structure maintained by tertiary ('kissing') interactions
Poly(rC) binding protein 2 binds to stem-loop IV of the poliovirus RNA 5' noncoding region: identification by automated liquid chromatography-tandem mass spectrometry
The cellular polypeptide p57 (pyrimidine tract-binding protein) binds to multiple sites in the poliovirus 5' nontranslated region
Minimum internal ribosome entry site required for poliovirus infectivity
Poliovirus RNA synthesis utilizes an RNP complex formed around the 5'-end of viral RNA
Towards identification of cis-acting elements involved in the replication of enterovirus and rhinovirus RNAs: a proposal for the existence of tRNA-like terminal structures
Intracellular modifications induced by poliovirus reduce the requirement for structural motifs in the 5' noncoding region of the genome involved in internal initiation of protein synthesis
Structural and functional analysis of the ribosome landing pad of poliovirus type 2: in vivo translation studies
A functional ribonucleoprotein complex forms around the 5' end of poliovirus RNA
A segment of the 5' nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation
Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA
In vitro translation of poliovirus RNA: utilization of internal initiation sites in reticulocyte lysate
Identification of the initiation site of poliovirus polyprotein synthesis
Carboxy-terminal analysis of poliovirus proteins: termination of poliovirus RNA translation and location of unique poliovirus polyprotein cleavage sites
Molecular cloning of poliovirus cDNA and determination of the complete nucleotide sequence of the viral genome
Primary structure, gene organization and polypeptide expression of poliovirus RNA
The genome-linked protein of picornaviruses. VII. Genetic mapping of poliovirus VPg by protein and RNA sequence studies
Sequence of 1060 3'-terminal nucleotides of poliovirus RNA as determined by a modification of the dideoxynucleotide method
Submitted (01-AUG-2000) National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA
REVIEWED REFSEQ: This record has been curated by NCBI staff. The\nreference sequence was derived from V01149.\nOn or before Jan 17, 2013 this sequence version replaced\nNC_001428.1, NC_014336.1, NC_002058.2.\nSee also entries V01148 (POLIO1A, for another version of this\ngenome) and V01150 (POLIOS1, for the genome of the Sabin 1 strain).\nSee the entry V01148 (POLIO1A) for the sequence reported in [3].\nMature peptides were added to the annotation by NCBI RefSeq Genomes\nstaff.\nCOMPLETENESS: full length.
The 5' non-translated region (NTR) harbors two functional domains, the cloverleaf and the internal ribosome entry site (IRES), and is covalently linked to the viral protein VPg.
EXISTENCE:site-directed mutagenesis and chemical and RNAase probing[ 2170027; 1310772]
Contains binding site for cellular poly(rC) binding protein 2 (PCBP2). Essential for RNA replication and, hence, viral prolifiration.
EXISTENCE:site-directed mutation[ 2170027; 20532207]
essential for the initiation of positive-strand RNA synthesis
EXISTENCE: site-directed mutagenesis and the crystal structure of a related protease[ 8253083 ]
binds poly(rC) binding protein 2 (PCBP2)
EXISTENCE:induced mutagenesis and deletion analysis[8230467]
involved in poliomavirus translation initiation and probably one of internal ribosome entry sites (IRES)
EXISTENCE:mutational analysis[ 8253083; 2170027; 9326487]
specifically interact with the viral proteinase and RNA binding protein 3CD pro
Contains C-rich region, nt 89-95, which is required for PCBP (cellular poly(C) binding proteins) to function as an essential cofactor in poliovirus genome.
EXISTENCE:immunoprecipitation, time course, and N-formyl-[35S]methionine labeling
IRES mediates cap-independent translation of the viral mRNA by facilitating initiation of translation independent of a capping group and a free 5' end.
interacts with pyrimidine tract-binding protein (PTB)
Essential for internal initiation of translation (showed experimentaly for Poliovirus 2).
EXISTENCE:automated liquid chromatography-tandem mass spectrometry[8855318]
binds with poly(rC) binding protein 2 (PCBP2)
EXISTENCE:The tethered hydroxyl-radical probing assays coupled with the mass spectrometry data.[20859255]
Stem-loop V binds single polypyrimidine tract-binding protein (PTB) in a unique orientation. PTB RNA-binding domains (RBDs) 1 and 2 interact with the basal part of Domain V, and RBDs3 and 4 binding the putatively single-stranded linkers flanking Domain V. This stimulates IRES activity by inducing eukaryotic translation initiation factor 4 gammaprotein (eIF4G) to bind in the optimal position and orientation to promote internal ribosome entry.
interacts with translation initiation factor 4 gammaprotein (eIF4G).
The polyprotein contains structural (P1) and non-structural (P2 and P3) proteins that are released from the polypeptide chain by proteolytic processing mediated by virally-encoded proteinases 2A pro and 3C pro/3CD pro to ultimately generate eleven mature viral proteins
EXISTENCE:Amino acid sequence analysis cleavage products of the polyprotein.[6264310]
Precursor of structural proteins. 3CDpro cleaves the P1 precursor polypeptide, giving rise to proteins VP0, VP3 and VP1.
Precursor of VP4 and VP2 capsid proteins. Cleavage of VP0 into capsid proteins VP4 and VP2 occurs during maturation of the virion.
EXISTENCE:x-ray crystallographic methods
Poliovirus capsid is formed from 60 copies of 4 coat protein subunits (VP1, VP2, VP3 and VP4). VP1, VP2 and VP3 are the major capsid proteins forming the icosahedral capsid shell (T=3), with a diameter of approximately 300 Angstroms. Each of them contains a 'core' consisting of an eight-stranded antiparallel beta barrel with two flanking helices. The capsid protects the viral genome from the environment, and facilitates delivery to appropriate target cells (by binding to the specific poliovirus receptor, PVR). As infection begins, viral RNA must be freed from the capsid during the 'uncoating' process and penetrate the cell. VP4 protein lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. Externalization of VP4 (together with N terminus of VP1 and shifts of the capsid beta barrels) initiates irreversible conformational change to the 135S particles ('A' particles) cell entry intermediate. It seems that Poliovirus enters different cells by different mechanisms, and point to a role for virus-induced intracellular signals in the process. PVR mediates virus attachment to target cells, initiates the uncoating process and inducts intracellular signals for virus entry.
EXISTENCE:x-ray crystallographic methods[2994218]
EXISTENCE:x-ray crystallographic methods[ 2994218]
EXISTENCE: x-ray crystallographic methods[2994218]
EXISTENCE:Amino acid sequence analysis and were found to be proteolytic cleavage products of the polyprotein.[6264310]
P2 precursor polypeptide is a precursor of nonstructural proteins, which is released from the polypeptide chain by proteolytic processing mediated by virally-encoded proteinases 2A pro to ultimately 3 mature viral proteins: 2A, 2B and 2C. P2 proteins are primarily responsible for the biochemical and structural changes that occur in the infected cell.
Picornain 2A (Protein 2A) is a small chymotrypsin-like cysteine proteinase. It is responsible for the cleavage between the P1 and P2 regions. In order to shut down the capped cellular mRNA transcription, picornain 2A cleaves the host translation initiation factor EIF4G1 and induces apoptotic cell death.
Processing of 2BC by 3Cpro gives rise to the mature products 2B and 2C, although a large fraction of 2BC remains uncleaved in picornavirus-infected cells. The expression of poliovirus 2BC protein in yeast and mammalian cells leads to a number of metabolic and morphological alterations, such as growth inhibition, intracellular membrane proliferation, blockade of the exocytic pathway, and enhanced membrane permeability.
Protein 2B enhances membrane permeability.
Involved in initiation and elongation of RNA synthesis, RNA encapsidation, virus uncoating and guanidine resistance (Asn179-Gly mutation). Putative helicase III.~2C protein (together with 2BC protein) induces the formation of host cell endoplasmic reticulum-derived rosette-like membranous structures, located in the cytoplasm, where the process of viral RNA replication takes place.
Processing of the P3 precursor occurs by two independent pathways, major and minor. In the major pathway, processing between 3B and 3C yields 3AB and 3CD. In the minor pathway, processing between 3A and 3B yields 3A and 3BCD. 3BCD processing yields 3BC and 3D; 3BC processing yields 3B and 3C.
EXISTENCE:Poliovirus polyprotein processing by the Gly-Gly mutant evaluated by Western blotting. [18779320]
Poliovirus protein 3AB displayes nucleic acid chaperone activity in promoting the hybridization of complementary nucleic acids and destabilizing secondary structure. It also stimulates the rate of binding between complementary nucleic acid, demonstrates helix-destabilizing activity, and serves as a donor for VPg uridylylation.
Poliovirus protein 3A is a small, membrane-binding protein that plays multiple roles in viral RNA replication complex formation and function. In the infected cell, this protein associates with other viral and cellular proteins as part of a supramolecular complex.
EXISTENCE:Poliovirus polyprotein processing by the Gly-Gly mutant evaluated by Western blotting.[18779320]
3BCD precursor protein is a precursor of 3BC and 3D proteins. Uncleaved precursor 3BCD is one of the substrates for uridylylation of VPg protein.
VPg (3B), a small protein that binds viral RNA and is necessary for synthesis of viral positive and negative strand RNA.
3CD protein lacks polymerase activity, but possesses protease activity with substrate recognition properties distinct from those of 3C protein. It was shown that cleavage of the viral capsid proteins, located in the N-terminal portion of the poliovirus polyprotein, requires 3CD-catalyzed proteolysis. 3CD protease activity has been implicated in cleavage of several host proteins. In addition to its proteolytic activities, 3CD also involved in viral RNA replication process. The protein binds to the cloverleaf structure at the 5? terminus of poliovirus RNA, and this binding was shown to be important for virus replication. 3CD also stimulates uridylylation of viral protein VPg, catalyzed by 3D, which is required for initiation of RNA replication, by binding to the template for uridylylation on the cis-acting replication element. 3CD protein interacts with the cellular heterogeneous nuclear ribonucleoprotein (hnRNP) C1/C2, which forms a specific RNP complex with the poliovirus 3? nontranslated region that is thought to be important for replication. 3CD (as well as another poliovirus protein, 3A), induces the recruitment to membranes of cellular proteins from the family of small GTPases, designated Arfs (ADP ribosylation factors).
Chymotrypsin-like cystein proteinase 3C. Viral 3C protease (3Cpro) plays a major role in translation regulation. It cleaves poly(A)-binding protein (PABP) and removes the C-terminal domain (CTD) that interacts with several translation factors. 3C protein has been shown to function as a stimulatory factor for 3Dpol in the VPg uridylylation reaction.
3D; The RNA-dependent RNA-polymerase, 3Dpol, is an essential component in genome for the replication of single stranded RNA. 3Dpol catalyze two independend half-reactions leading to the attachment of VPg protein to the 5' end of viral RNA. First, VPg is uridylylated to produce VPg-pUpU; second, VPg-pUpU serves as a primer for full-length RNA synthesis
The genomic RNA 3' noncoding region is believed to be a major cis-acting molecular genetic determinant for regulating picornavirus negative-strand RNA synthesis by promoting replication complex recognition. This region predicted to exhibit conserved secondary structures consisting of two stem-loops: X and Y. Furthermore, a proposed tertiary 'kissing' interaction involving base pairing between the loop regions of stem-loops X and Y was suggested.