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Article

The Influenza Virus RNA-Polymerase and the Host RNA-Polymerase II: RPB4 Is Targeted by a PB2 Domain That Is Involved in Viral Transcription

1
Unité de Virologie et Immunologie Moléculaires, INRAE, Université Paris-Saclay, 78350 Jouy-en-Josas, France
2
Biological Adaptation and Ageing (B2A), Institut de Biologie Paris-Seine (IBPS), Sorbonne Université, CNRS, 75005 Paris, France
*
Author to whom correspondence should be addressed.
Academic Editor: Ayato Takada
Viruses 2022, 14(3), 518; https://doi.org/10.3390/v14030518
Received: 1 February 2022 / Revised: 28 February 2022 / Accepted: 1 March 2022 / Published: 3 March 2022
(This article belongs to the Section Animal Viruses)
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 influenza A 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 was found to occur with the homologous domains of influenza B and C FluPols. The N-half domain of RPB4 was found to be critical in this interaction. Punctual mutants generated at conserved positions between influenza A, B, and C FluPols in the N-third domain of PB2 exhibited strong transcriptional activity defects. These results suggest that FluPol interacts with several domains of Pol II (the CTD to bind Pol II), initiating host transcription and a second transcription on RPB4 to locate FluPol at the proximity of the 5′-end of nascent host mRNA. View Full-Text
Keywords: influenza virus; RNA-polymerase; RNA-polymerase II; protein-protein interaction; PPI; cap snatching; transcription; binary complementation assay influenza virus; RNA-polymerase; RNA-polymerase II; protein-protein interaction; PPI; cap snatching; transcription; binary complementation assay
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MDPI and ACS Style

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. Viruses 2022, 14, 518. https://doi.org/10.3390/v14030518

AMA Style

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. Viruses. 2022; 14(3):518. https://doi.org/10.3390/v14030518

Chicago/Turabian Style

Morel, Jessica, Laura Sedano, Nathalie Lejal, Bruno Da Costa, Eric Batsché, 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" Viruses 14, no. 3: 518. https://doi.org/10.3390/v14030518

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