tetano
Editor, Senior Moderator
J Mol Biol
. 2022 Jan 21;167460.
doi: 10.1016/j.jmb.2022.167460. Online ahead of print.
PABP1 Drives the Selective Translation of Influenza A Virus mRNA
Cyrus M de Rozières[SUP] 1 [/SUP], Alberto Pequeno[SUP] 1 [/SUP], Shandy Shahabi[SUP] 1 [/SUP], Taryn M Lucas[SUP] 1 [/SUP], Kamil Godula[SUP] 1 [/SUP], Gourisankar Ghosh[SUP] 1 [/SUP], Simpson Joseph[SUP] 2 [/SUP]
Affiliations
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.
Keywords: Eukaryotic Initiation Factor 4G; Poly(A) binding protein; RT-qPCR; anisotropy; immunoprecipitation.
. 2022 Jan 21;167460.
doi: 10.1016/j.jmb.2022.167460. Online ahead of print.
PABP1 Drives the Selective Translation of Influenza A Virus mRNA
Cyrus M de Rozières[SUP] 1 [/SUP], Alberto Pequeno[SUP] 1 [/SUP], Shandy Shahabi[SUP] 1 [/SUP], Taryn M Lucas[SUP] 1 [/SUP], Kamil Godula[SUP] 1 [/SUP], Gourisankar Ghosh[SUP] 1 [/SUP], Simpson Joseph[SUP] 2 [/SUP]
Affiliations
- PMID: 35074482
- DOI: 10.1016/j.jmb.2022.167460
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.
Keywords: Eukaryotic Initiation Factor 4G; Poly(A) binding protein; RT-qPCR; anisotropy; immunoprecipitation.