Self-capping of nucleoprotein filaments protects the Newcastle disease virus genome

Non-segmented negative-strand RNA viruses, such as measles, ebola and Newcastle disease viruses (NDV), encapsidate viral genomic RNAs into helical nucleocapsids, which serve as the template for viral replication and transcription. Here, the clam-shaped nucleocapsid structure, where the NDV viral gen...

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Main Authors: Xiyong Song, Hong Shan, Yanping Zhu, Shunlin Hu, Ling Xue, Yong Chen, Wei Ding, Tongxin Niu, Jian Gu, Songying Ouyang, Qing-Tao Shen, Zhi-Jie Liu
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2019-07-01
Series:eLife
Subjects:
Online Access:https://elifesciences.org/articles/45057
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spelling doaj-762128936a9b4a708d05c893c009c9642021-05-05T17:45:42ZengeLife Sciences Publications LtdeLife2050-084X2019-07-01810.7554/eLife.45057Self-capping of nucleoprotein filaments protects the Newcastle disease virus genomeXiyong Song0https://orcid.org/0000-0002-5088-3783Hong Shan1Yanping Zhu2Shunlin Hu3Ling Xue4Yong Chen5Wei Ding6Tongxin Niu7Jian Gu8Songying Ouyang9Qing-Tao Shen10Zhi-Jie Liu11https://orcid.org/0000-0001-7279-2893Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming, China; National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China; College of Life Sciences, University of Chinese Academy of Sciences, Beijing, ChinaiHuman Institute, ShanghaiTech University, Shanghai, ChinaNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou, ChinaNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China; College of Life Sciences, University of Chinese Academy of Sciences, Beijing, ChinaCenter for Biological Imaging, Institute of Biophysics, Chinese Academy of Sciences, Beijing, ChinaCenter for Biological Imaging, Institute of Biophysics, Chinese Academy of Sciences, Beijing, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou, ChinaThe Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of Ministry of Education, College of Life Sciences, Fujian Normal University, Fuzhou, China; Provincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, College of Life Sciences, Fujian Normal University, Fuzhou, ChinaiHuman Institute, ShanghaiTech University, Shanghai, ChinaInstitute of Molecular and Clinical Medicine, Kunming Medical University, Kunming, China; National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China; iHuman Institute, ShanghaiTech University, Shanghai, ChinaNon-segmented negative-strand RNA viruses, such as measles, ebola and Newcastle disease viruses (NDV), encapsidate viral genomic RNAs into helical nucleocapsids, which serve as the template for viral replication and transcription. Here, the clam-shaped nucleocapsid structure, where the NDV viral genome is sequestered, was determined at 4.8 Å resolution by cryo-electron microscopy. The clam-shaped structure is composed of two single-turn spirals packed in a back-to-back mode. This tightly packed structure functions as a seed for the assembly of a nucleocapsid from both directions, facilitating the growth of double-headed filaments with two separate RNA strings inside. Disruption of this structure by mutations in its loop interface yielded a single-headed unfunctional filament.https://elifesciences.org/articles/45057cryo-electron microscopyclam-like shaped structurefilamentnewcastle disease virus
collection DOAJ
language English
format Article
sources DOAJ
author Xiyong Song
Hong Shan
Yanping Zhu
Shunlin Hu
Ling Xue
Yong Chen
Wei Ding
Tongxin Niu
Jian Gu
Songying Ouyang
Qing-Tao Shen
Zhi-Jie Liu
spellingShingle Xiyong Song
Hong Shan
Yanping Zhu
Shunlin Hu
Ling Xue
Yong Chen
Wei Ding
Tongxin Niu
Jian Gu
Songying Ouyang
Qing-Tao Shen
Zhi-Jie Liu
Self-capping of nucleoprotein filaments protects the Newcastle disease virus genome
eLife
cryo-electron microscopy
clam-like shaped structure
filament
newcastle disease virus
author_facet Xiyong Song
Hong Shan
Yanping Zhu
Shunlin Hu
Ling Xue
Yong Chen
Wei Ding
Tongxin Niu
Jian Gu
Songying Ouyang
Qing-Tao Shen
Zhi-Jie Liu
author_sort Xiyong Song
title Self-capping of nucleoprotein filaments protects the Newcastle disease virus genome
title_short Self-capping of nucleoprotein filaments protects the Newcastle disease virus genome
title_full Self-capping of nucleoprotein filaments protects the Newcastle disease virus genome
title_fullStr Self-capping of nucleoprotein filaments protects the Newcastle disease virus genome
title_full_unstemmed Self-capping of nucleoprotein filaments protects the Newcastle disease virus genome
title_sort self-capping of nucleoprotein filaments protects the newcastle disease virus genome
publisher eLife Sciences Publications Ltd
series eLife
issn 2050-084X
publishDate 2019-07-01
description Non-segmented negative-strand RNA viruses, such as measles, ebola and Newcastle disease viruses (NDV), encapsidate viral genomic RNAs into helical nucleocapsids, which serve as the template for viral replication and transcription. Here, the clam-shaped nucleocapsid structure, where the NDV viral genome is sequestered, was determined at 4.8 Å resolution by cryo-electron microscopy. The clam-shaped structure is composed of two single-turn spirals packed in a back-to-back mode. This tightly packed structure functions as a seed for the assembly of a nucleocapsid from both directions, facilitating the growth of double-headed filaments with two separate RNA strings inside. Disruption of this structure by mutations in its loop interface yielded a single-headed unfunctional filament.
topic cryo-electron microscopy
clam-like shaped structure
filament
newcastle disease virus
url https://elifesciences.org/articles/45057
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