Version 1
: Received: 10 February 2022 / Approved: 14 February 2022 / Online: 14 February 2022 (09:51:21 CET)
How to cite:
Morel, J.; Sedano, L.; Lejal, N.; Da Costa, B.; Batsché, E.; Muchardt, C.; Delmas, B. The Influenza Virus RNA-polymerase and the Host RNA-Polymerase II: RPB4 is Targeted by a PB2 Domain that is Involved in Viral Transcription. Preprints2022, 2022020170. https://doi.org/10.20944/preprints202202.0170.v1
Morel, J.; Sedano, L.; Lejal, N.; Da Costa, B.; Batsché, E.; Muchardt, C.; Delmas, B. The Influenza Virus RNA-polymerase and the Host RNA-Polymerase II: RPB4 is Targeted by a PB2 Domain that is Involved in Viral Transcription. Preprints 2022, 2022020170. https://doi.org/10.20944/preprints202202.0170.v1
Morel, J.; Sedano, L.; Lejal, N.; Da Costa, B.; Batsché, E.; Muchardt, C.; Delmas, B. The Influenza Virus RNA-polymerase and the Host RNA-Polymerase II: RPB4 is Targeted by a PB2 Domain that is Involved in Viral Transcription. Preprints2022, 2022020170. https://doi.org/10.20944/preprints202202.0170.v1
APA Style
Morel, J., Sedano, L., Lejal, N., Da Costa, B., Batsché, E., Muchardt, C., & Delmas, B. (2022). The Influenza Virus RNA-polymerase and the Host RNA-Polymerase II: RPB4 is Targeted by a PB2 Domain that is Involved in Viral Transcription. Preprints. https://doi.org/10.20944/preprints202202.0170.v1
Chicago/Turabian Style
Morel, J., Christian Muchardt and Bernard Delmas. 2022 "The Influenza Virus RNA-polymerase and the Host RNA-Polymerase II: RPB4 is Targeted by a PB2 Domain that is Involved in Viral Transcription" Preprints. https://doi.org/10.20944/preprints202202.0170.v1
Abstract
Influenza virus transcription is catalyzed by the viral RNA-polymerase (FluPol) through a cap-snatching activity. The snatching of the cap of cellular mRNA by FluPol is preceded by its binding to the flexible C-terminal domain (CTD) of the RPB1 subunit of RNA-polymerase II (Pol II). To better understand how FluPol brings the 3’-end of the genomic RNAs in close proximity to the host-derived primer, we hypothesized that FluPol may recognize additional Pol II subunits/domains to ensure cap-snatching. Using binary complementation assays between the Pol II and FluPol subunits and their structural domains, we revealed an interaction between the N-third domain of PB2 and RPB4. This interaction was confirmed by a co-immunoprecipitation assay and found to occur with the homologous domains of influenza B and C FluPols. Residues [1-72] of RPB4 were found critical in this interaction. Numerous punctual mutants generated at conserved positions between influenza A, B and C FluPols in the N-third domain of PB2 exhibited strong transcriptional activity defect. These results suggest that FluPol interacts with several domains/subunits of Pol II, the CTD to bind Pol II initiating host transcription and a second on RPB4 to locate FluPol at the proximity of the 5’-end of nascent host mRNA.
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
