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Details on Person Spliced and unspliced viral mRNA in the cytoplasm are transl...

Class:IdSummation:195587
_displayNameSpliced and unspliced viral mRNA in the cytoplasm are transl...
_timestamp2007-04-09 18:37:05
created[InstanceEdit:195595] Gillespie, ME, 2007-04-09 18:36:45
literatureReference[LiteratureReference:192798] The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanism
[LiteratureReference:192709] Effects of influenza A virus NS1 protein on protein expression: the NS1 protein enhances translation and is not required for shutoff of host protein synthesis
[LiteratureReference:192640] PABP1 and eIF4GI associate with influenza virus NS1 protein in viral mRNA translation initiation complexes
[LiteratureReference:192902] Regulation of eukaryotic protein synthesis: selective influenza viral mRNA translation is mediated by the cellular RNA-binding protein GRSF-1
[LiteratureReference:192861] Translational control by influenza virus. Identification of cis-acting sequences and trans-acting factors which may regulate selective viral mRNA translation.
[LiteratureReference:192790] Selective translation of eukaryotic mRNAs: functional molecular analysis of GRSF-1, a positive regulator of influenza virus protein synthesis
[LiteratureReference:169181] A novel influenza A virus mitochondrial protein that induces cell death
[LiteratureReference:192730] Cellular mRNA translation is blocked at both initiation and elongation after infection by influenza virus or adenovirus
[LiteratureReference:192641] Translational control by influenza virus. Selective and cap-dependent translation of viral mRNAs in infected cells.
textSpliced and unspliced viral mRNA in the cytoplasm are translated by host cell ribosomal translation machinery (reviewed in Kash, 2006). At least ten viral proteins are synthesized: HA, NA, PB1, PB2, PA, NP, NS1, NEP/NS2, M1, and M2. Viral mRNA translation is believed to be enhanced by conserved 5'UTR sequences that interact with the ribosomal machinery and at least one cellular RNA-binding protein, G-rich sequence factor 1 (GRSF-1), has been found to specifically interact with the viral 5’UTRs. (Park, 1995; Park, 1999). The viral NS1 protein and the cellular protein P58(IPK) enhance viral translation indirectly by preventing the activation of the translational inhibitor PKR (Salvatore, 2002; Goodman, 2006). The viral NS1 protein has also been proposed to specifically enhance translation through interaction with host poly(A)-binding protein 1 (PABP1) (Burgui, 2003). Simultaneously, host cell protein synthesis is downregulated in influenza virus infection through still uncharacterized mechanisms (Katze, 1986; Garfinkel, 1992; Kash, 2006). In most human influenza A strains (such as PR8), the PB1 mRNA segment is capable of producing a second protein, PB1-F2, from a short +1 open reading frame initiating downstream of the of the PB1 ORF initiation codon (Chen, 2001).
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