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Towards an atomic resolution understanding of the influenza virus replication machinery Volume 14, issue 6, novembre-décembre 2010

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Authors
UMI 3265 UJF-EMBL-CNRS, Biologie structurale des interactions entre virus et cellule hôte, 6, rue Jules-Horowitz, BP 181, 38042 Grenoble cedex 09, France, EMBL, antenne de Grenoble, 6, rue Jules-Horowitz, BP 181, 38042 Grenoble cedex 09, France

Influenza virus polymerase transcribes and replicates the viral RNA genome within the context of a ribonucleoprotein complex that has been hitherto remarkably intractable to structural analysis. In the last three years, crystal structures of independent domains covering roughly half of the hetero-trimeric polymerase have been determined. These include the cap-binding and endonuclease domains, critical for the unique cap-snatching mechanism of mRNA transcription, and the major inter-subunit interfaces. In addition a cryo-electron microscopy structure of the entire ribonucleoprotein complex has been determined opening the way to the construction of a quasi-atomic model of the influenza replication machinery. These results provide the first detailed structure-function insights into polymerase assembly, transcription and host adaptation and will have an impact on anti-influenza drug design.