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            <funder>This work was funded by the ANR grant FluTranscript (ANR-18-CE11-0028, S.C. and N.N.), the ANR LabEx IBEID (ANR-10-LABX-62-IBEID, N.N. and T.K.), and the German Research Foundation (DFG) grant SFB-TR84 (project B2, T.W.). This work used the platforms at the Grenoble Instruct-ERIC Center (ISBG; UMS 3518 CNRS CEA-UGA-EMBL) with support from the French Infrastructure for Integrated Structural Biology (FRISBI; ANR-10-INSB-05-02) and GRAL, a project of the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003) within the GrenoblePartnership for Structural Biology. The IBS Electron Microscope facility is supported by the Auvergne Rhône-Alpes Region, the Fonds Feder, the Fondation pour la Recherche Médicale and GIS-IBiSA.</funder>
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            <idno type="halRefHtml">&lt;i&gt;Nature Communications&lt;/i&gt;, 2024, 15 (1), pp.1064. &lt;a target="_blank" href="https://dx.doi.org/10.1038/s41467-024-45205-2"&gt;&amp;#x27E8;10.1038/s41467-024-45205-2&amp;#x27E9;&lt;/a&gt;</idno>
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                <title xml:lang="en">The host RNA polymerase II C-terminal domain is the anchor for replication of the influenza virus genome</title>
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                    <forename type="first">Thorsten</forename>
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                <title level="j">Nature Communications</title>
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                  <publisher>Nature Publishing Group</publisher>
                  <biblScope unit="volume">15</biblScope>
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              <p>Abstract The current model is that the influenza virus polymerase (FluPol) binds either to host RNA polymerase II (RNAP II) or to the acidic nuclear phosphoprotein 32 (ANP32), which drives its conformation and activity towards transcription or replication of the viral genome, respectively. Here, we provide evidence that the FluPol-RNAP II binding interface, beyond its well-acknowledged function in cap-snatching during transcription initiation, has also a pivotal role in replication of the viral genome. Using a combination of cell-based and in vitro approaches, we show that the RNAP II C-terminal-domain, jointly with ANP32, enhances FluPol replication activity. We observe successive conformational changes to switch from a transcriptase to a replicase conformation in the presence of the bound RNPAII C-terminal domain and propose a model in which the host RNAP II is the anchor for transcription and replication of the viral genome. Our data open new perspectives on the spatial coupling of viral transcription and replication and the coordinated balance between these two activities.</p>
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              <org type="consortium">We thank Ron Fouchier (Erasmus MC Department of Viroscience, Netherlands), George Brownlee (Oxford University), Bernard Delmas (INRAE, France), Robert-Jan Lebbink (Utrecht University, Netherlands) and Sandie Munier (Institut Pasteur, France) for sharing plasmids and antibodies. We thank Martin Pelosse for support in using the Eukaryotic Expression Facility at EMBL Grenoble; Aldo R. Camacho-Zarco and Martin Blackledge for providing huANP32A truncated constructs pro- teins; Daphne Walter and Vladimir Benes from the EMBL GeneCore facility for the next generation sequencing data; Wojtek Galej, Sarah Schneider and Romain Linares for access to the Glacios at EMBL Gre- noble; Guy Schoehn and Eleftherios Zarkadas for access to the Glacios at IBS Grenoble; Aymeric Peuch for support with using the joint EMBL- IBS computer clusters. We acknowledge the European Synchrotron Radiation Facility and PSB for access to the Titan Krios CM01, and Michael Hons for assistance with data collection. We thank the Pasteur International Bioresources Network (PIBNet) for genome sequencing of recombinant viruses.</org>
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