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N-terminal basic amino acid residues of Beet black scorch virus capsid protein play a critical role in virion assembly and systemic movement
BACKGROUND: Beet black scorch virus (BBSV) is a small single-stranded, positive-sense RNA plant virus belonging to the genus Necrovirus, family Tombusviridae. Its capsid protein (CP) contains a 13 amino acid long basic region at the N-terminus, rich in arginine and lysine residues, which is thought...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3691604/ https://www.ncbi.nlm.nih.gov/pubmed/23786675 http://dx.doi.org/10.1186/1743-422X-10-200 |
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author | Zhang, Xiaofeng Zhao, Xiaofei Zhang, Yanjing Niu, Shaofang Qu, Feng Zhang, Yongliang Han, Chenggui Yu, Jialin Li, Dawei |
author_facet | Zhang, Xiaofeng Zhao, Xiaofei Zhang, Yanjing Niu, Shaofang Qu, Feng Zhang, Yongliang Han, Chenggui Yu, Jialin Li, Dawei |
author_sort | Zhang, Xiaofeng |
collection | PubMed |
description | BACKGROUND: Beet black scorch virus (BBSV) is a small single-stranded, positive-sense RNA plant virus belonging to the genus Necrovirus, family Tombusviridae. Its capsid protein (CP) contains a 13 amino acid long basic region at the N-terminus, rich in arginine and lysine residues, which is thought to interact with viral RNA to initiate virion assembly. RESULTS: In the current study, a series of BBSV mutants containing amino acid substitutions as well as deletions within the N-terminal region were generated and examined for their effects on viral RNA replication, virion assembly, and long distance spread in protoplasts and whole host plants of BBSV. The RNA-binding activities of the mutated CPs were also evaluated in vitro. These experiments allowed us to identify two key basic amino acid residues in this region that are responsible for initiating virus assembly through RNA-binding. Proper assembly of BBSV particles is in turn needed for efficient viral systemic movement. CONCLUSIONS: We have identified two basic amino acid residues near the N-terminus of the BBSV CP that bind viral RNA with high affinity to initiate virion assembly. We further provide evidence showing that systemic spread of BBSV in infected plants requires intact virions. This study represents the first in-depth investigation of the role of basic amino acid residues within the N-terminus of a necroviral CP. |
format | Online Article Text |
id | pubmed-3691604 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-36916042013-06-26 N-terminal basic amino acid residues of Beet black scorch virus capsid protein play a critical role in virion assembly and systemic movement Zhang, Xiaofeng Zhao, Xiaofei Zhang, Yanjing Niu, Shaofang Qu, Feng Zhang, Yongliang Han, Chenggui Yu, Jialin Li, Dawei Virol J Research BACKGROUND: Beet black scorch virus (BBSV) is a small single-stranded, positive-sense RNA plant virus belonging to the genus Necrovirus, family Tombusviridae. Its capsid protein (CP) contains a 13 amino acid long basic region at the N-terminus, rich in arginine and lysine residues, which is thought to interact with viral RNA to initiate virion assembly. RESULTS: In the current study, a series of BBSV mutants containing amino acid substitutions as well as deletions within the N-terminal region were generated and examined for their effects on viral RNA replication, virion assembly, and long distance spread in protoplasts and whole host plants of BBSV. The RNA-binding activities of the mutated CPs were also evaluated in vitro. These experiments allowed us to identify two key basic amino acid residues in this region that are responsible for initiating virus assembly through RNA-binding. Proper assembly of BBSV particles is in turn needed for efficient viral systemic movement. CONCLUSIONS: We have identified two basic amino acid residues near the N-terminus of the BBSV CP that bind viral RNA with high affinity to initiate virion assembly. We further provide evidence showing that systemic spread of BBSV in infected plants requires intact virions. This study represents the first in-depth investigation of the role of basic amino acid residues within the N-terminus of a necroviral CP. BioMed Central 2013-06-20 /pmc/articles/PMC3691604/ /pubmed/23786675 http://dx.doi.org/10.1186/1743-422X-10-200 Text en Copyright © 2013 Zhang et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Zhang, Xiaofeng Zhao, Xiaofei Zhang, Yanjing Niu, Shaofang Qu, Feng Zhang, Yongliang Han, Chenggui Yu, Jialin Li, Dawei N-terminal basic amino acid residues of Beet black scorch virus capsid protein play a critical role in virion assembly and systemic movement |
title | N-terminal basic amino acid residues of Beet black scorch virus capsid protein play a critical role in virion assembly and systemic movement |
title_full | N-terminal basic amino acid residues of Beet black scorch virus capsid protein play a critical role in virion assembly and systemic movement |
title_fullStr | N-terminal basic amino acid residues of Beet black scorch virus capsid protein play a critical role in virion assembly and systemic movement |
title_full_unstemmed | N-terminal basic amino acid residues of Beet black scorch virus capsid protein play a critical role in virion assembly and systemic movement |
title_short | N-terminal basic amino acid residues of Beet black scorch virus capsid protein play a critical role in virion assembly and systemic movement |
title_sort | n-terminal basic amino acid residues of beet black scorch virus capsid protein play a critical role in virion assembly and systemic movement |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3691604/ https://www.ncbi.nlm.nih.gov/pubmed/23786675 http://dx.doi.org/10.1186/1743-422X-10-200 |
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