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CryoEM structure of the Nipah virus nucleocapsid assembly

Nipah and its close relative Hendra are highly pathogenic zoonotic viruses, storing their ssRNA genome in a helical nucleocapsid assembly formed by the N protein, a major viral immunogen. Here, we report the first cryoEM structure for a Henipavirus RNA-bound nucleocapsid assembly, at 3.5 Å resolutio...

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Autores principales: Ker, De-Sheng, Jenkins, Huw T., Greive, Sandra J., Antson, Alfred A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8318291/
https://www.ncbi.nlm.nih.gov/pubmed/34270629
http://dx.doi.org/10.1371/journal.ppat.1009740
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author Ker, De-Sheng
Jenkins, Huw T.
Greive, Sandra J.
Antson, Alfred A.
author_facet Ker, De-Sheng
Jenkins, Huw T.
Greive, Sandra J.
Antson, Alfred A.
author_sort Ker, De-Sheng
collection PubMed
description Nipah and its close relative Hendra are highly pathogenic zoonotic viruses, storing their ssRNA genome in a helical nucleocapsid assembly formed by the N protein, a major viral immunogen. Here, we report the first cryoEM structure for a Henipavirus RNA-bound nucleocapsid assembly, at 3.5 Å resolution. The helical assembly is stabilised by previously undefined N- and C-terminal segments, contributing to subunit-subunit interactions. RNA is wrapped around the nucleocapsid protein assembly with a periodicity of six nucleotides per protomer, in the “3-bases-in, 3-bases-out” conformation, with protein plasticity enabling non-sequence specific interactions. The structure reveals commonalities in RNA binding pockets and in the conformation of bound RNA, not only with members of the Paramyxoviridae family, but also with the evolutionarily distant Filoviridae Ebola virus. Significant structural differences with other Paramyxoviridae members are also observed, particularly in the position and length of the exposed α-helix, residues 123–139, which may serve as a valuable epitope for surveillance and diagnostics.
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spelling pubmed-83182912021-07-31 CryoEM structure of the Nipah virus nucleocapsid assembly Ker, De-Sheng Jenkins, Huw T. Greive, Sandra J. Antson, Alfred A. PLoS Pathog Research Article Nipah and its close relative Hendra are highly pathogenic zoonotic viruses, storing their ssRNA genome in a helical nucleocapsid assembly formed by the N protein, a major viral immunogen. Here, we report the first cryoEM structure for a Henipavirus RNA-bound nucleocapsid assembly, at 3.5 Å resolution. The helical assembly is stabilised by previously undefined N- and C-terminal segments, contributing to subunit-subunit interactions. RNA is wrapped around the nucleocapsid protein assembly with a periodicity of six nucleotides per protomer, in the “3-bases-in, 3-bases-out” conformation, with protein plasticity enabling non-sequence specific interactions. The structure reveals commonalities in RNA binding pockets and in the conformation of bound RNA, not only with members of the Paramyxoviridae family, but also with the evolutionarily distant Filoviridae Ebola virus. Significant structural differences with other Paramyxoviridae members are also observed, particularly in the position and length of the exposed α-helix, residues 123–139, which may serve as a valuable epitope for surveillance and diagnostics. Public Library of Science 2021-07-16 /pmc/articles/PMC8318291/ /pubmed/34270629 http://dx.doi.org/10.1371/journal.ppat.1009740 Text en © 2021 Ker et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Ker, De-Sheng
Jenkins, Huw T.
Greive, Sandra J.
Antson, Alfred A.
CryoEM structure of the Nipah virus nucleocapsid assembly
title CryoEM structure of the Nipah virus nucleocapsid assembly
title_full CryoEM structure of the Nipah virus nucleocapsid assembly
title_fullStr CryoEM structure of the Nipah virus nucleocapsid assembly
title_full_unstemmed CryoEM structure of the Nipah virus nucleocapsid assembly
title_short CryoEM structure of the Nipah virus nucleocapsid assembly
title_sort cryoem structure of the nipah virus nucleocapsid assembly
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8318291/
https://www.ncbi.nlm.nih.gov/pubmed/34270629
http://dx.doi.org/10.1371/journal.ppat.1009740
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