<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Marion Declercq</style></author><author><style face="normal" font="default" size="100%">Elise Biquand</style></author><author><style face="normal" font="default" size="100%">Marwah Karim</style></author><author><style face="normal" font="default" size="100%">Natalia Pietrosemoli</style></author><author><style face="normal" font="default" size="100%">Yves Jacob</style></author><author><style face="normal" font="default" size="100%">Caroline Demeret</style></author><author><style face="normal" font="default" size="100%">Cyril Barbezange</style></author><author><style face="normal" font="default" size="100%">Sylvie van der Werf</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Influenza A virus co-opts ERI1 exonuclease bound to histone mRNA to promote viral transcription.</style></title><secondary-title><style face="normal" font="default" size="100%">Nucleic Acids Res</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Exoribonucleases</style></keyword><keyword><style  face="normal" font="default" size="100%">Histones</style></keyword><keyword><style  face="normal" font="default" size="100%">Host-Pathogen Interactions</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Influenza A virus</style></keyword><keyword><style  face="normal" font="default" size="100%">Influenza, Human</style></keyword><keyword><style  face="normal" font="default" size="100%">mRNA Cleavage and Polyadenylation Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Nuclear Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Ribonucleoproteins</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA Stability</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Messenger</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Small Interfering</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Transcription, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Viral Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Replication</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2020</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2020 10 09</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">48</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Cellular exonucleases involved in the processes that regulate RNA stability and quality control have been shown to restrict or to promote the multiplication cycle of numerous RNA viruses. Influenza A viruses are major human pathogens that are responsible for seasonal epidemics, but the interplay between viral proteins and cellular exonucleases has never been specifically studied. Here, using a stringent interactomics screening strategy and an siRNA-silencing approach, we identified eight cellular factors among a set of 75 cellular proteins carrying exo(ribo)nuclease activities or involved in RNA decay processes that support influenza A virus multiplication. We show that the exoribonuclease ERI1 interacts with the PB2, PB1 and NP components of the viral ribonucleoproteins and is required for viral mRNA transcription. More specifically, we demonstrate that the protein-protein interaction is RNA dependent and that both the RNA binding and exonuclease activities of ERI1 are required to promote influenza A virus transcription. Finally, we provide evidence that during infection, the SLBP protein and histone mRNAs co-purify with vRNPs alongside ERI1, indicating that ERI1 is most probably recruited when it is present in the histone pre-mRNA processing complex in the nucleus.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">18</style></issue></record></records></xml>