Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.

In contrast to most RNA viruses, influenza viruses replicate their genome in the nucleus of infected cells. As a result, newly-synthesized vRNA genomes, in the form of viral ribonucleoprotein complexes (vRNPs), must be exported to the cytoplasm for productive infection. To characterize the compositi...

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Autores principales:	Geoffrey P Chase, Marie-Anne Rameix-Welti, Aurelija Zvirbliene, Gintautas Zvirblis, Veronika Götz, Thorsten Wolff, Nadia Naffakh, Martin Schwemmle
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/68310bef0de84cffa627d438a764ca72
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spelling	oai:doaj.org-article:68310bef0de84cffa627d438a764ca722021-11-18T06:03:03ZInfluenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.1553-73661553-737410.1371/journal.ppat.1002187https://doaj.org/article/68310bef0de84cffa627d438a764ca722011-09-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21909257/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374In contrast to most RNA viruses, influenza viruses replicate their genome in the nucleus of infected cells. As a result, newly-synthesized vRNA genomes, in the form of viral ribonucleoprotein complexes (vRNPs), must be exported to the cytoplasm for productive infection. To characterize the composition of vRNP export complexes and their interplay with the nucleus of infected cells, we affinity-purified tagged vRNPs from biochemically fractionated infected nuclei. After treatment of infected cells with leptomycin B, a potent inhibitor of Crm1-mediated export, we isolated vRNP export complexes which, unexpectedly, were tethered to the host-cell chromatin with very high affinity. At late time points of infection, the cellular export receptor Crm1 also accumulated at the same regions of the chromatin as vRNPs, which led to a decrease in the export of other nuclear Crm1 substrates from the nucleus. Interestingly, chromatin targeting of vRNP export complexes brought them into association with Rcc1, the Ran guanine exchange factor responsible for generating RanGTP and driving Crm1-dependent nuclear export. Thus, influenza viruses gain preferential access to newly-generated host cell export machinery by targeting vRNP export complexes at the sites of Ran regeneration.Geoffrey P ChaseMarie-Anne Rameix-WeltiAurelija ZvirblieneGintautas ZvirblisVeronika GötzThorsten WolffNadia NaffakhMartin SchwemmlePublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 7, Iss 9, p e1002187 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Geoffrey P Chase Marie-Anne Rameix-Welti Aurelija Zvirbliene Gintautas Zvirblis Veronika Götz Thorsten Wolff Nadia Naffakh Martin Schwemmle Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.
description	In contrast to most RNA viruses, influenza viruses replicate their genome in the nucleus of infected cells. As a result, newly-synthesized vRNA genomes, in the form of viral ribonucleoprotein complexes (vRNPs), must be exported to the cytoplasm for productive infection. To characterize the composition of vRNP export complexes and their interplay with the nucleus of infected cells, we affinity-purified tagged vRNPs from biochemically fractionated infected nuclei. After treatment of infected cells with leptomycin B, a potent inhibitor of Crm1-mediated export, we isolated vRNP export complexes which, unexpectedly, were tethered to the host-cell chromatin with very high affinity. At late time points of infection, the cellular export receptor Crm1 also accumulated at the same regions of the chromatin as vRNPs, which led to a decrease in the export of other nuclear Crm1 substrates from the nucleus. Interestingly, chromatin targeting of vRNP export complexes brought them into association with Rcc1, the Ran guanine exchange factor responsible for generating RanGTP and driving Crm1-dependent nuclear export. Thus, influenza viruses gain preferential access to newly-generated host cell export machinery by targeting vRNP export complexes at the sites of Ran regeneration.
format	article
author	Geoffrey P Chase Marie-Anne Rameix-Welti Aurelija Zvirbliene Gintautas Zvirblis Veronika Götz Thorsten Wolff Nadia Naffakh Martin Schwemmle
author_facet	Geoffrey P Chase Marie-Anne Rameix-Welti Aurelija Zvirbliene Gintautas Zvirblis Veronika Götz Thorsten Wolff Nadia Naffakh Martin Schwemmle
author_sort	Geoffrey P Chase
title	Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.
title_short	Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.
title_full	Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.
title_fullStr	Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.
title_full_unstemmed	Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.
title_sort	influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/68310bef0de84cffa627d438a764ca72
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Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.

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