Rab18 binds to classical swine fever virus NS5A and mediates viral replication and assembly in swine umbilical vein endothelial cells

Classical swine fever virus (CSFV), a positive-sense RNA virus, hijacks cell host proteins for its own replication. Rab18, a small Rab GTPase, regulates intracellular membrane-trafficking events between various compartments in cells and is involved in the life cycle of multiple viruses. However, the...

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Autores principales:	Liang Zhang, Di Zhao, Mingxing Jin, Mengzhao Song, Shanchuan Liu, Kangkang Guo, Yanming Zhang
Formato:	article
Lenguaje:	EN
Publicado:	Taylor & Francis Group 2020
Materias:	classical swine fever virus rab18 ns5a interaction replication assembly Infectious and parasitic diseases RC109-216
Acceso en línea:	https://doaj.org/article/a5b02eacfc5c4cae80266f5e1e8088ab
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spelling	oai:doaj.org-article:a5b02eacfc5c4cae80266f5e1e8088ab2021-11-17T14:21:58ZRab18 binds to classical swine fever virus NS5A and mediates viral replication and assembly in swine umbilical vein endothelial cells2150-55942150-560810.1080/21505594.2020.1767356https://doaj.org/article/a5b02eacfc5c4cae80266f5e1e8088ab2020-12-01T00:00:00Zhttp://dx.doi.org/10.1080/21505594.2020.1767356https://doaj.org/toc/2150-5594https://doaj.org/toc/2150-5608Classical swine fever virus (CSFV), a positive-sense RNA virus, hijacks cell host proteins for its own replication. Rab18, a small Rab GTPase, regulates intracellular membrane-trafficking events between various compartments in cells and is involved in the life cycle of multiple viruses. However, the effect of Rab18 on the production of CSFV remains uncertain. In this study, we showed that knockdown of Rab18 by lentiviruses inhibited CSFV production, while overexpression of Rab18 by lentiviruses enhanced CSFV production. Subsequent experiments revealed that the negative-mutant Rab18-S22 N inhibited CSFV infection, while the positive-mutant Rab18-Q67 L enhanced CSFV infection. Furthermore, we showed that CSFV RNA replication and virion assembly, measured by real-time fluorescence quantitative PCR (RT-qPCR), indirect immunofluorescence assay (IFA), and confocal microscopy, were reduced in cells lacking Rab18 expression. In addition, co-immunoprecipitation, GST-pulldown, and confocal microscopy assays revealed that Rab18 bound to the viral protein NS5A. Further, NS5A was shown to be redistributed in Rab18 knockdown cells. Taken together, these findings demonstrate Rab18 as a novel host factor required for CSFV RNA replication and particle assembly by interaction with the viral protein NS5A.Liang ZhangDi ZhaoMingxing JinMengzhao SongShanchuan LiuKangkang GuoYanming ZhangTaylor & Francis Grouparticleclassical swine fever virusrab18ns5ainteractionreplicationassemblyInfectious and parasitic diseasesRC109-216ENVirulence, Vol 11, Iss 1, Pp 489-501 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	classical swine fever virus rab18 ns5a interaction replication assembly Infectious and parasitic diseases RC109-216
spellingShingle	classical swine fever virus rab18 ns5a interaction replication assembly Infectious and parasitic diseases RC109-216 Liang Zhang Di Zhao Mingxing Jin Mengzhao Song Shanchuan Liu Kangkang Guo Yanming Zhang Rab18 binds to classical swine fever virus NS5A and mediates viral replication and assembly in swine umbilical vein endothelial cells
description	Classical swine fever virus (CSFV), a positive-sense RNA virus, hijacks cell host proteins for its own replication. Rab18, a small Rab GTPase, regulates intracellular membrane-trafficking events between various compartments in cells and is involved in the life cycle of multiple viruses. However, the effect of Rab18 on the production of CSFV remains uncertain. In this study, we showed that knockdown of Rab18 by lentiviruses inhibited CSFV production, while overexpression of Rab18 by lentiviruses enhanced CSFV production. Subsequent experiments revealed that the negative-mutant Rab18-S22 N inhibited CSFV infection, while the positive-mutant Rab18-Q67 L enhanced CSFV infection. Furthermore, we showed that CSFV RNA replication and virion assembly, measured by real-time fluorescence quantitative PCR (RT-qPCR), indirect immunofluorescence assay (IFA), and confocal microscopy, were reduced in cells lacking Rab18 expression. In addition, co-immunoprecipitation, GST-pulldown, and confocal microscopy assays revealed that Rab18 bound to the viral protein NS5A. Further, NS5A was shown to be redistributed in Rab18 knockdown cells. Taken together, these findings demonstrate Rab18 as a novel host factor required for CSFV RNA replication and particle assembly by interaction with the viral protein NS5A.
format	article
author	Liang Zhang Di Zhao Mingxing Jin Mengzhao Song Shanchuan Liu Kangkang Guo Yanming Zhang
author_facet	Liang Zhang Di Zhao Mingxing Jin Mengzhao Song Shanchuan Liu Kangkang Guo Yanming Zhang
author_sort	Liang Zhang
title	Rab18 binds to classical swine fever virus NS5A and mediates viral replication and assembly in swine umbilical vein endothelial cells
title_short	Rab18 binds to classical swine fever virus NS5A and mediates viral replication and assembly in swine umbilical vein endothelial cells
title_full	Rab18 binds to classical swine fever virus NS5A and mediates viral replication and assembly in swine umbilical vein endothelial cells
title_fullStr	Rab18 binds to classical swine fever virus NS5A and mediates viral replication and assembly in swine umbilical vein endothelial cells
title_full_unstemmed	Rab18 binds to classical swine fever virus NS5A and mediates viral replication and assembly in swine umbilical vein endothelial cells
title_sort	rab18 binds to classical swine fever virus ns5a and mediates viral replication and assembly in swine umbilical vein endothelial cells
publisher	Taylor & Francis Group
publishDate	2020
url	https://doaj.org/article/a5b02eacfc5c4cae80266f5e1e8088ab
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Rab18 binds to classical swine fever virus NS5A and mediates viral replication and assembly in swine umbilical vein endothelial cells

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