| Literature DB >> 35074482 |
Cyrus M de Rozières1, Alberto Pequeno1, Shandy Shahabi1, Taryn M Lucas1, Kamil Godula1, Gourisankar Ghosh1, Simpson Joseph2.
Abstract
Influenza A virus (IAV) is a human-infecting pathogen with a history of causing seasonal epidemics and on several occasions worldwide pandemics. Infection by IAV causes a dramatic decrease in host mRNA translation, whereas viral mRNAs are efficiently translated. The IAV mRNAs have a highly conserved 5'-untranslated region (5'UTR) that is rich in adenosine residues. We show that the human polyadenylate binding protein 1 (PABP1) binds to the 5'UTR of the viral mRNAs. The interaction of PABP1 with the viral 5'UTR makes the translation of viral mRNAs more resistant to canonical cap-dependent translation inhibition than model mRNAs. Additionally, PABP1 bound to the viral 5'UTR can recruit eIF4G in an eIF4E-independent manner. These results indicate that PABP1 bound to the viral 5'UTR may promote eIF4E-independent translation initiation.Entities:
Keywords: RT-qPCR; anisotropy; eukaryotic initiation factor 4G; immunoprecipitation; poly(A) binding protein
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Year: 2022 PMID: 35074482 PMCID: PMC8897273 DOI: 10.1016/j.jmb.2022.167460
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469