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Nucleocapsid Structure of Negative Strand RNA Virus
Negative strand RNA viruses (NSVs) include many important human pathogens, such as influenza virus, Ebola virus, and rabies virus. One of the unique characteristics that NSVs share is the assembly of the nucleocapsid and its role in viral RNA synthesis. In NSVs, the single strand RNA genome is encap...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7472042/ https://www.ncbi.nlm.nih.gov/pubmed/32751700 http://dx.doi.org/10.3390/v12080835 |
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author | Luo, Ming Terrell, James Ross Mcmanus, Shelby Ashlyn |
author_facet | Luo, Ming Terrell, James Ross Mcmanus, Shelby Ashlyn |
author_sort | Luo, Ming |
collection | PubMed |
description | Negative strand RNA viruses (NSVs) include many important human pathogens, such as influenza virus, Ebola virus, and rabies virus. One of the unique characteristics that NSVs share is the assembly of the nucleocapsid and its role in viral RNA synthesis. In NSVs, the single strand RNA genome is encapsidated in the linear nucleocapsid throughout the viral replication cycle. Subunits of the nucleocapsid protein are parallelly aligned along the RNA genome that is sandwiched between two domains composed of conserved helix motifs. The viral RNA-dependent-RNA polymerase (vRdRp) must recognize the protein–RNA complex of the nucleocapsid and unveil the protected genomic RNA in order to initiate viral RNA synthesis. In addition, vRdRp must continuously translocate along the protein–RNA complex during elongation in viral RNA synthesis. This unique mechanism of viral RNA synthesis suggests that the nucleocapsid may play a regulatory role during NSV replication. |
format | Online Article Text |
id | pubmed-7472042 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-74720422020-09-17 Nucleocapsid Structure of Negative Strand RNA Virus Luo, Ming Terrell, James Ross Mcmanus, Shelby Ashlyn Viruses Review Negative strand RNA viruses (NSVs) include many important human pathogens, such as influenza virus, Ebola virus, and rabies virus. One of the unique characteristics that NSVs share is the assembly of the nucleocapsid and its role in viral RNA synthesis. In NSVs, the single strand RNA genome is encapsidated in the linear nucleocapsid throughout the viral replication cycle. Subunits of the nucleocapsid protein are parallelly aligned along the RNA genome that is sandwiched between two domains composed of conserved helix motifs. The viral RNA-dependent-RNA polymerase (vRdRp) must recognize the protein–RNA complex of the nucleocapsid and unveil the protected genomic RNA in order to initiate viral RNA synthesis. In addition, vRdRp must continuously translocate along the protein–RNA complex during elongation in viral RNA synthesis. This unique mechanism of viral RNA synthesis suggests that the nucleocapsid may play a regulatory role during NSV replication. MDPI 2020-07-30 /pmc/articles/PMC7472042/ /pubmed/32751700 http://dx.doi.org/10.3390/v12080835 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Luo, Ming Terrell, James Ross Mcmanus, Shelby Ashlyn Nucleocapsid Structure of Negative Strand RNA Virus |
title | Nucleocapsid Structure of Negative Strand RNA Virus |
title_full | Nucleocapsid Structure of Negative Strand RNA Virus |
title_fullStr | Nucleocapsid Structure of Negative Strand RNA Virus |
title_full_unstemmed | Nucleocapsid Structure of Negative Strand RNA Virus |
title_short | Nucleocapsid Structure of Negative Strand RNA Virus |
title_sort | nucleocapsid structure of negative strand rna virus |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7472042/ https://www.ncbi.nlm.nih.gov/pubmed/32751700 http://dx.doi.org/10.3390/v12080835 |
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