Role of PDZ-binding motif from West Nile virus NS5 protein on viral replication

Abstract West Nile virus (WNV) is a Flavivirus, which can cause febrile illness in humans that may progress to encephalitis. Like any other obligate intracellular pathogens, Flaviviruses hijack cellular protein functions as a strategy for sustaining their life cycle. Many cellular proteins display g...

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Autores principales:	Emilie Giraud, Chloé Otero del Val, Célia Caillet-Saguy, Nada Zehrouni, Cécile Khou, Joël Caillet, Yves Jacob, Nathalie Pardigon, Nicolas Wolff
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/116840311ac24ecf9d4b8f395299d86d
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spelling	oai:doaj.org-article:116840311ac24ecf9d4b8f395299d86d2021-12-02T10:44:15ZRole of PDZ-binding motif from West Nile virus NS5 protein on viral replication10.1038/s41598-021-82751-x2045-2322https://doaj.org/article/116840311ac24ecf9d4b8f395299d86d2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-82751-xhttps://doaj.org/toc/2045-2322Abstract West Nile virus (WNV) is a Flavivirus, which can cause febrile illness in humans that may progress to encephalitis. Like any other obligate intracellular pathogens, Flaviviruses hijack cellular protein functions as a strategy for sustaining their life cycle. Many cellular proteins display globular domain known as PDZ domain that interacts with PDZ-Binding Motifs (PBM) identified in many viral proteins. Thus, cellular PDZ-containing proteins are common targets during viral infection. The non-structural protein 5 (NS5) from WNV provides both RNA cap methyltransferase and RNA polymerase activities and is involved in viral replication but its interactions with host proteins remain poorly known. In this study, we demonstrate that the C-terminal PBM of WNV NS5 recognizes several human PDZ-containing proteins using both in vitro and in cellulo high-throughput methods. Furthermore, we constructed and assayed in cell culture WNV replicons where the PBM within NS5 was mutated. Our results demonstrate that the PBM of WNV NS5 is important in WNV replication. Moreover, we show that knockdown of the PDZ-containing proteins TJP1, PARD3, ARHGAP21 or SHANK2 results in the decrease of WNV replication in cells. Altogether, our data reveal that interactions between the PBM of NS5 and PDZ-containing proteins affect West Nile virus replication.Emilie GiraudChloé Otero del ValCélia Caillet-SaguyNada ZehrouniCécile KhouJoël CailletYves JacobNathalie PardigonNicolas WolffNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Emilie Giraud Chloé Otero del Val Célia Caillet-Saguy Nada Zehrouni Cécile Khou Joël Caillet Yves Jacob Nathalie Pardigon Nicolas Wolff Role of PDZ-binding motif from West Nile virus NS5 protein on viral replication
description	Abstract West Nile virus (WNV) is a Flavivirus, which can cause febrile illness in humans that may progress to encephalitis. Like any other obligate intracellular pathogens, Flaviviruses hijack cellular protein functions as a strategy for sustaining their life cycle. Many cellular proteins display globular domain known as PDZ domain that interacts with PDZ-Binding Motifs (PBM) identified in many viral proteins. Thus, cellular PDZ-containing proteins are common targets during viral infection. The non-structural protein 5 (NS5) from WNV provides both RNA cap methyltransferase and RNA polymerase activities and is involved in viral replication but its interactions with host proteins remain poorly known. In this study, we demonstrate that the C-terminal PBM of WNV NS5 recognizes several human PDZ-containing proteins using both in vitro and in cellulo high-throughput methods. Furthermore, we constructed and assayed in cell culture WNV replicons where the PBM within NS5 was mutated. Our results demonstrate that the PBM of WNV NS5 is important in WNV replication. Moreover, we show that knockdown of the PDZ-containing proteins TJP1, PARD3, ARHGAP21 or SHANK2 results in the decrease of WNV replication in cells. Altogether, our data reveal that interactions between the PBM of NS5 and PDZ-containing proteins affect West Nile virus replication.
format	article
author	Emilie Giraud Chloé Otero del Val Célia Caillet-Saguy Nada Zehrouni Cécile Khou Joël Caillet Yves Jacob Nathalie Pardigon Nicolas Wolff
author_facet	Emilie Giraud Chloé Otero del Val Célia Caillet-Saguy Nada Zehrouni Cécile Khou Joël Caillet Yves Jacob Nathalie Pardigon Nicolas Wolff
author_sort	Emilie Giraud
title	Role of PDZ-binding motif from West Nile virus NS5 protein on viral replication
title_short	Role of PDZ-binding motif from West Nile virus NS5 protein on viral replication
title_full	Role of PDZ-binding motif from West Nile virus NS5 protein on viral replication
title_fullStr	Role of PDZ-binding motif from West Nile virus NS5 protein on viral replication
title_full_unstemmed	Role of PDZ-binding motif from West Nile virus NS5 protein on viral replication
title_sort	role of pdz-binding motif from west nile virus ns5 protein on viral replication
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/116840311ac24ecf9d4b8f395299d86d
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Role of PDZ-binding motif from West Nile virus NS5 protein on viral replication

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