Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers

Abstract Coronaviruses (CoV) are enveloped viruses and rely on their nucleocapsid N protein to incorporate the positive-stranded genomic RNA into the virions. CoV N proteins form oligomers but the mechanism and relevance underlying their multimerization remain to be fully understood. Using in vitro...

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Autores principales:	Yingying Cong, Franziska Kriegenburg, Cornelis A. M. de Haan, Fulvio Reggiori
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1bd9db3283e34102b0ac19f4492e089d
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spelling	oai:doaj.org-article:1bd9db3283e34102b0ac19f4492e089d2021-12-02T12:31:59ZCoronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers10.1038/s41598-017-06062-w2045-2322https://doaj.org/article/1bd9db3283e34102b0ac19f4492e089d2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06062-whttps://doaj.org/toc/2045-2322Abstract Coronaviruses (CoV) are enveloped viruses and rely on their nucleocapsid N protein to incorporate the positive-stranded genomic RNA into the virions. CoV N proteins form oligomers but the mechanism and relevance underlying their multimerization remain to be fully understood. Using in vitro pull-down experiments and density glycerol gradients, we found that at least 3 regions distributed over its entire length mediate the self-interaction of mouse hepatitis virus (MHV) and severe acute respiratory syndrome coronavirus (SARS-CoV) N protein. The fact that these regions can bind reciprocally between themselves provides a possible molecular basis for N protein oligomerization. Interestingly, cytoplasmic N molecules of MHV-infected cells constitutively assemble into oligomers through a process that does not require binding to genomic RNA. Based on our data, we propose a model where constitutive N protein oligomerization allows the optimal loading of the genomic viral RNA into a ribonucleoprotein complex via the presentation of multiple viral RNA binding motifs.Yingying CongFranziska KriegenburgCornelis A. M. de HaanFulvio ReggioriNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Yingying Cong Franziska Kriegenburg Cornelis A. M. de Haan Fulvio Reggiori Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers
description	Abstract Coronaviruses (CoV) are enveloped viruses and rely on their nucleocapsid N protein to incorporate the positive-stranded genomic RNA into the virions. CoV N proteins form oligomers but the mechanism and relevance underlying their multimerization remain to be fully understood. Using in vitro pull-down experiments and density glycerol gradients, we found that at least 3 regions distributed over its entire length mediate the self-interaction of mouse hepatitis virus (MHV) and severe acute respiratory syndrome coronavirus (SARS-CoV) N protein. The fact that these regions can bind reciprocally between themselves provides a possible molecular basis for N protein oligomerization. Interestingly, cytoplasmic N molecules of MHV-infected cells constitutively assemble into oligomers through a process that does not require binding to genomic RNA. Based on our data, we propose a model where constitutive N protein oligomerization allows the optimal loading of the genomic viral RNA into a ribonucleoprotein complex via the presentation of multiple viral RNA binding motifs.
format	article
author	Yingying Cong Franziska Kriegenburg Cornelis A. M. de Haan Fulvio Reggiori
author_facet	Yingying Cong Franziska Kriegenburg Cornelis A. M. de Haan Fulvio Reggiori
author_sort	Yingying Cong
title	Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers
title_short	Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers
title_full	Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers
title_fullStr	Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers
title_full_unstemmed	Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers
title_sort	coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/1bd9db3283e34102b0ac19f4492e089d
work_keys_str_mv	AT yingyingcong coronavirusnucleocapsidproteinsassembleconstitutivelyinhighmolecularoligomers AT franziskakriegenburg coronavirusnucleocapsidproteinsassembleconstitutivelyinhighmolecularoligomers AT cornelisamdehaan coronavirusnucleocapsidproteinsassembleconstitutivelyinhighmolecularoligomers AT fulvioreggiori coronavirusnucleocapsidproteinsassembleconstitutivelyinhighmolecularoligomers
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Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers

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