Loading…
The Influenza Virus RNA-Polymerase and the Host RNA-Polymerase II: RPB4 Is Targeted by a PB2 Domain That Is Involved in Viral Transcription
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 unders...
Saved in:
Published in: | Viruses 2022-03, Vol.14 (3), p.518 |
---|---|
Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c503t-c395d2c72a4ce2bbbb4133e7b89c01bd4441ae170f014307de6278364752207c3 |
---|---|
cites | cdi_FETCH-LOGICAL-c503t-c395d2c72a4ce2bbbb4133e7b89c01bd4441ae170f014307de6278364752207c3 |
container_end_page | |
container_issue | 3 |
container_start_page | 518 |
container_title | Viruses |
container_volume | 14 |
creator | Morel, Jessica Sedano, Laura Lejal, Nathalie Da Costa, Bruno Batsché, Eric Muchardt, Christian Delmas, Bernard |
description | 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. |
doi_str_mv | 10.3390/v14030518 |
format | article |
fullrecord | <record><control><sourceid>proquest_doaj_</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_de39a1df99b148c1a6f46eff01f67a2d</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_de39a1df99b148c1a6f46eff01f67a2d</doaj_id><sourcerecordid>2642488211</sourcerecordid><originalsourceid>FETCH-LOGICAL-c503t-c395d2c72a4ce2bbbb4133e7b89c01bd4441ae170f014307de6278364752207c3</originalsourceid><addsrcrecordid>eNpdkt1u0zAUgCMEYmNwwQsgS9zARcB_sWMuJnUb0EgVVFPg1nIcp02V2MVOInWvwEvj0lG2-sbWOZ-_42OdJHmN4AdCBPw4IQoJzFD-JDlHQoiUCpQ9fXA-S16EsIGQMQH58-SMZIQwgbPz5He5NqCwTTcae6fAz9aPAdx-m6VL1-1641UwQNkaDBGbuzCc5oriE7hdXlFQBFAqvzKDqUG1AwosrzC4cb1qLSjXatgDhZ1cN0UgxmIl1YHSKxu0b7dD6-zL5FmjumBe3e8XyY8vn8vrebr4_rW4ni1SnUEypJqIrMaaY0W1wVVcFBFieJULDVFVU0qRMojDBiJKIK8NwzwnjPIMY8g1uUiKg7d2aiO3vu2V30mnWvk34PxKKj-0ujOyNkQoVDdCVIjmGinWUGaaaG4YV7iOrsuDaztWvam1sUPs65H0cca2a7lyk8xFBhHGUfD-IFifXJvPFnIfg4QhxjGdUGTf3Rfz7tdowiD7NmjTdcoaNwaJGaUwNg3ziL49QTdu9DZ-657CNM8xQv-La-9C8KY5vgBBuR8teRytyL552OmR_DdL5A-jwMYU</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2642488211</pqid></control><display><type>article</type><title>The Influenza Virus RNA-Polymerase and the Host RNA-Polymerase II: RPB4 Is Targeted by a PB2 Domain That Is Involved in Viral Transcription</title><source>Publicly Available Content (ProQuest)</source><source>PubMed Central</source><creator>Morel, Jessica ; Sedano, Laura ; Lejal, Nathalie ; Da Costa, Bruno ; Batsché, Eric ; Muchardt, Christian ; Delmas, Bernard</creator><creatorcontrib>Morel, Jessica ; Sedano, Laura ; Lejal, Nathalie ; Da Costa, Bruno ; Batsché, Eric ; Muchardt, Christian ; Delmas, Bernard</creatorcontrib><description>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.</description><identifier>ISSN: 1999-4915</identifier><identifier>EISSN: 1999-4915</identifier><identifier>DOI: 10.3390/v14030518</identifier><identifier>PMID: 35336925</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino acids ; Binding sites ; cap snatching ; Cloning ; Complementation ; DNA-directed RNA polymerase ; Genomes ; Humans ; Immunoprecipitation ; Influenza ; Influenza A ; Influenza B ; influenza virus ; Influenza, Human ; Life Sciences ; Microbiology and Parasitology ; Mutagenesis ; Mutation ; Orthomyxoviridae - genetics ; Plasmids ; PPI ; protein-protein interaction ; Proteins ; RNA Polymerase II - metabolism ; RNA viruses ; RNA, Messenger - genetics ; RNA, Viral - genetics ; RNA, Viral - metabolism ; RNA-Dependent RNA Polymerase - genetics ; RNA-polymerase ; RNA-polymerase II ; Transcription ; Viral Transcription ; Virology ; Virus Replication ; Viruses</subject><ispartof>Viruses, 2022-03, Vol.14 (3), p.518</ispartof><rights>2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Attribution</rights><rights>2022 by the authors. 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c503t-c395d2c72a4ce2bbbb4133e7b89c01bd4441ae170f014307de6278364752207c3</citedby><cites>FETCH-LOGICAL-c503t-c395d2c72a4ce2bbbb4133e7b89c01bd4441ae170f014307de6278364752207c3</cites><orcidid>0000-0003-0145-4023 ; 0000-0002-5145-5270 ; 0000-0002-2978-6823</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2642488211/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2642488211?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35336925$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://uvsq.hal.science/hal-03616724$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Morel, Jessica</creatorcontrib><creatorcontrib>Sedano, Laura</creatorcontrib><creatorcontrib>Lejal, Nathalie</creatorcontrib><creatorcontrib>Da Costa, Bruno</creatorcontrib><creatorcontrib>Batsché, Eric</creatorcontrib><creatorcontrib>Muchardt, Christian</creatorcontrib><creatorcontrib>Delmas, Bernard</creatorcontrib><title>The Influenza Virus RNA-Polymerase and the Host RNA-Polymerase II: RPB4 Is Targeted by a PB2 Domain That Is Involved in Viral Transcription</title><title>Viruses</title><addtitle>Viruses</addtitle><description>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.</description><subject>Amino acids</subject><subject>Binding sites</subject><subject>cap snatching</subject><subject>Cloning</subject><subject>Complementation</subject><subject>DNA-directed RNA polymerase</subject><subject>Genomes</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Influenza</subject><subject>Influenza A</subject><subject>Influenza B</subject><subject>influenza virus</subject><subject>Influenza, Human</subject><subject>Life Sciences</subject><subject>Microbiology and Parasitology</subject><subject>Mutagenesis</subject><subject>Mutation</subject><subject>Orthomyxoviridae - genetics</subject><subject>Plasmids</subject><subject>PPI</subject><subject>protein-protein interaction</subject><subject>Proteins</subject><subject>RNA Polymerase II - metabolism</subject><subject>RNA viruses</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Viral - genetics</subject><subject>RNA, Viral - metabolism</subject><subject>RNA-Dependent RNA Polymerase - genetics</subject><subject>RNA-polymerase</subject><subject>RNA-polymerase II</subject><subject>Transcription</subject><subject>Viral Transcription</subject><subject>Virology</subject><subject>Virus Replication</subject><subject>Viruses</subject><issn>1999-4915</issn><issn>1999-4915</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNpdkt1u0zAUgCMEYmNwwQsgS9zARcB_sWMuJnUb0EgVVFPg1nIcp02V2MVOInWvwEvj0lG2-sbWOZ-_42OdJHmN4AdCBPw4IQoJzFD-JDlHQoiUCpQ9fXA-S16EsIGQMQH58-SMZIQwgbPz5He5NqCwTTcae6fAz9aPAdx-m6VL1-1641UwQNkaDBGbuzCc5oriE7hdXlFQBFAqvzKDqUG1AwosrzC4cb1qLSjXatgDhZ1cN0UgxmIl1YHSKxu0b7dD6-zL5FmjumBe3e8XyY8vn8vrebr4_rW4ni1SnUEypJqIrMaaY0W1wVVcFBFieJULDVFVU0qRMojDBiJKIK8NwzwnjPIMY8g1uUiKg7d2aiO3vu2V30mnWvk34PxKKj-0ujOyNkQoVDdCVIjmGinWUGaaaG4YV7iOrsuDaztWvam1sUPs65H0cca2a7lyk8xFBhHGUfD-IFifXJvPFnIfg4QhxjGdUGTf3Rfz7tdowiD7NmjTdcoaNwaJGaUwNg3ziL49QTdu9DZ-657CNM8xQv-La-9C8KY5vgBBuR8teRytyL552OmR_DdL5A-jwMYU</recordid><startdate>20220303</startdate><enddate>20220303</enddate><creator>Morel, Jessica</creator><creator>Sedano, Laura</creator><creator>Lejal, Nathalie</creator><creator>Da Costa, Bruno</creator><creator>Batsché, Eric</creator><creator>Muchardt, Christian</creator><creator>Delmas, Bernard</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0003-0145-4023</orcidid><orcidid>https://orcid.org/0000-0002-5145-5270</orcidid><orcidid>https://orcid.org/0000-0002-2978-6823</orcidid></search><sort><creationdate>20220303</creationdate><title>The Influenza Virus RNA-Polymerase and the Host RNA-Polymerase II: RPB4 Is Targeted by a PB2 Domain That Is Involved in Viral Transcription</title><author>Morel, Jessica ; Sedano, Laura ; Lejal, Nathalie ; Da Costa, Bruno ; Batsché, Eric ; Muchardt, Christian ; Delmas, Bernard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c503t-c395d2c72a4ce2bbbb4133e7b89c01bd4441ae170f014307de6278364752207c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Amino acids</topic><topic>Binding sites</topic><topic>cap snatching</topic><topic>Cloning</topic><topic>Complementation</topic><topic>DNA-directed RNA polymerase</topic><topic>Genomes</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Influenza</topic><topic>Influenza A</topic><topic>Influenza B</topic><topic>influenza virus</topic><topic>Influenza, Human</topic><topic>Life Sciences</topic><topic>Microbiology and Parasitology</topic><topic>Mutagenesis</topic><topic>Mutation</topic><topic>Orthomyxoviridae - genetics</topic><topic>Plasmids</topic><topic>PPI</topic><topic>protein-protein interaction</topic><topic>Proteins</topic><topic>RNA Polymerase II - metabolism</topic><topic>RNA viruses</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Viral - genetics</topic><topic>RNA, Viral - metabolism</topic><topic>RNA-Dependent RNA Polymerase - genetics</topic><topic>RNA-polymerase</topic><topic>RNA-polymerase II</topic><topic>Transcription</topic><topic>Viral Transcription</topic><topic>Virology</topic><topic>Virus Replication</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Morel, Jessica</creatorcontrib><creatorcontrib>Sedano, Laura</creatorcontrib><creatorcontrib>Lejal, Nathalie</creatorcontrib><creatorcontrib>Da Costa, Bruno</creatorcontrib><creatorcontrib>Batsché, Eric</creatorcontrib><creatorcontrib>Muchardt, Christian</creatorcontrib><creatorcontrib>Delmas, Bernard</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Biological Science Database</collection><collection>Publicly Available Content (ProQuest)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Directory of Open Access Journals</collection><jtitle>Viruses</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Morel, Jessica</au><au>Sedano, Laura</au><au>Lejal, Nathalie</au><au>Da Costa, Bruno</au><au>Batsché, Eric</au><au>Muchardt, Christian</au><au>Delmas, Bernard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Influenza Virus RNA-Polymerase and the Host RNA-Polymerase II: RPB4 Is Targeted by a PB2 Domain That Is Involved in Viral Transcription</atitle><jtitle>Viruses</jtitle><addtitle>Viruses</addtitle><date>2022-03-03</date><risdate>2022</risdate><volume>14</volume><issue>3</issue><spage>518</spage><pages>518-</pages><issn>1999-4915</issn><eissn>1999-4915</eissn><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 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.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>35336925</pmid><doi>10.3390/v14030518</doi><orcidid>https://orcid.org/0000-0003-0145-4023</orcidid><orcidid>https://orcid.org/0000-0002-5145-5270</orcidid><orcidid>https://orcid.org/0000-0002-2978-6823</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1999-4915 |
ispartof | Viruses, 2022-03, Vol.14 (3), p.518 |
issn | 1999-4915 1999-4915 |
language | eng |
recordid | cdi_doaj_primary_oai_doaj_org_article_de39a1df99b148c1a6f46eff01f67a2d |
source | Publicly Available Content (ProQuest); PubMed Central |
subjects | Amino acids Binding sites cap snatching Cloning Complementation DNA-directed RNA polymerase Genomes Humans Immunoprecipitation Influenza Influenza A Influenza B influenza virus Influenza, Human Life Sciences Microbiology and Parasitology Mutagenesis Mutation Orthomyxoviridae - genetics Plasmids PPI protein-protein interaction Proteins RNA Polymerase II - metabolism RNA viruses RNA, Messenger - genetics RNA, Viral - genetics RNA, Viral - metabolism RNA-Dependent RNA Polymerase - genetics RNA-polymerase RNA-polymerase II Transcription Viral Transcription Virology Virus Replication Viruses |
title | The Influenza Virus RNA-Polymerase and the Host RNA-Polymerase II: RPB4 Is Targeted by a PB2 Domain That Is Involved in Viral Transcription |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T04%3A39%3A46IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_doaj_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Influenza%20Virus%20RNA-Polymerase%20and%20the%20Host%20RNA-Polymerase%20II:%20RPB4%20Is%20Targeted%20by%20a%20PB2%20Domain%20That%20Is%20Involved%20in%20Viral%20Transcription&rft.jtitle=Viruses&rft.au=Morel,%20Jessica&rft.date=2022-03-03&rft.volume=14&rft.issue=3&rft.spage=518&rft.pages=518-&rft.issn=1999-4915&rft.eissn=1999-4915&rft_id=info:doi/10.3390/v14030518&rft_dat=%3Cproquest_doaj_%3E2642488211%3C/proquest_doaj_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c503t-c395d2c72a4ce2bbbb4133e7b89c01bd4441ae170f014307de6278364752207c3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2642488211&rft_id=info:pmid/35336925&rfr_iscdi=true |