Negative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D pol

Abstract Most single stranded plus RNA viruses hijack phosphatidylinositol 4-kinases (PI4Ks) to generate membranes highly enriched in phosphatidylinositol 4-phosphate (PI4P). These membranous compartments known as webs, replication factories or replication organelles are essential for viral replicat...

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Autores principales:	Anna Dubankova, Jana Humpolickova, Martin Klima, Evzen Boura
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/84d3484b6a7343a2ab7fed6472212864
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spelling	oai:doaj.org-article:84d3484b6a7343a2ab7fed64722128642021-12-02T15:06:06ZNegative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D pol10.1038/s41598-017-17621-62045-2322https://doaj.org/article/84d3484b6a7343a2ab7fed64722128642017-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-17621-6https://doaj.org/toc/2045-2322Abstract Most single stranded plus RNA viruses hijack phosphatidylinositol 4-kinases (PI4Ks) to generate membranes highly enriched in phosphatidylinositol 4-phosphate (PI4P). These membranous compartments known as webs, replication factories or replication organelles are essential for viral replication because they provide protection from the innate intracellular immune response while serving as platforms for viral replication. Using purified recombinant proteins and biomimetic model membranes we show that the nonstructural viral 3A protein is sufficient to promote membrane hyper-phosphorylation given the proper intracellular cofactors (PI4KB and ACBD3). However, our bio-mimetic in vitro reconstitution assay revealed that rather than the presence of PI4P specifically, negative charge alone is sufficient for the recruitment of 3Dpol enzymes to the surface of the lipid bilayer. Additionally, we show that membrane tethered viral 3B protein (also known as Vpg) works in combination with the negative charge to increase the efficiency of membrane recruitment of 3Dpol.Anna DubankovaJana HumpolickovaMartin KlimaEvzen BouraNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Anna Dubankova Jana Humpolickova Martin Klima Evzen Boura Negative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D pol
description	Abstract Most single stranded plus RNA viruses hijack phosphatidylinositol 4-kinases (PI4Ks) to generate membranes highly enriched in phosphatidylinositol 4-phosphate (PI4P). These membranous compartments known as webs, replication factories or replication organelles are essential for viral replication because they provide protection from the innate intracellular immune response while serving as platforms for viral replication. Using purified recombinant proteins and biomimetic model membranes we show that the nonstructural viral 3A protein is sufficient to promote membrane hyper-phosphorylation given the proper intracellular cofactors (PI4KB and ACBD3). However, our bio-mimetic in vitro reconstitution assay revealed that rather than the presence of PI4P specifically, negative charge alone is sufficient for the recruitment of 3Dpol enzymes to the surface of the lipid bilayer. Additionally, we show that membrane tethered viral 3B protein (also known as Vpg) works in combination with the negative charge to increase the efficiency of membrane recruitment of 3Dpol.
format	article
author	Anna Dubankova Jana Humpolickova Martin Klima Evzen Boura
author_facet	Anna Dubankova Jana Humpolickova Martin Klima Evzen Boura
author_sort	Anna Dubankova
title	Negative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D pol
title_short	Negative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D pol
title_full	Negative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D pol
title_fullStr	Negative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D pol
title_full_unstemmed	Negative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D pol
title_sort	negative charge and membrane-tethered viral 3b cooperate to recruit viral rna dependent rna polymerase 3d pol
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/84d3484b6a7343a2ab7fed6472212864
work_keys_str_mv	AT annadubankova negativechargeandmembranetetheredviral3bcooperatetorecruitviralrnadependentrnapolymerase3dpol AT janahumpolickova negativechargeandmembranetetheredviral3bcooperatetorecruitviralrnadependentrnapolymerase3dpol AT martinklima negativechargeandmembranetetheredviral3bcooperatetorecruitviralrnadependentrnapolymerase3dpol AT evzenboura negativechargeandmembranetetheredviral3bcooperatetorecruitviralrnadependentrnapolymerase3dpol
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Negative charge and membrane-tethered viral 3B cooperate to recruit viral RNA dependent RNA polymerase 3D pol

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