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Cryo-EM Structure of a Begomovirus Geminate Particle

Tobacco curly shoot virus, a monopartite begomovirus associated with betasatellite, causes serious leaf curl diseases on tomato and tobacco in China. Using single-particle cryo-electron microscopy, we determined the structure of tobacco curly shoot virus (TbCSV) particle at 3.57 Å resolution and con...

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Detalles Bibliográficos
Autores principales: Xu, Xiongbiao, Zhang, Qing, Hong, Jian, Li, Zhenghe, Zhang, Xiaokang, Zhou, Xueping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6480954/
https://www.ncbi.nlm.nih.gov/pubmed/30965627
http://dx.doi.org/10.3390/ijms20071738
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author Xu, Xiongbiao
Zhang, Qing
Hong, Jian
Li, Zhenghe
Zhang, Xiaokang
Zhou, Xueping
author_facet Xu, Xiongbiao
Zhang, Qing
Hong, Jian
Li, Zhenghe
Zhang, Xiaokang
Zhou, Xueping
author_sort Xu, Xiongbiao
collection PubMed
description Tobacco curly shoot virus, a monopartite begomovirus associated with betasatellite, causes serious leaf curl diseases on tomato and tobacco in China. Using single-particle cryo-electron microscopy, we determined the structure of tobacco curly shoot virus (TbCSV) particle at 3.57 Å resolution and confirmed the characteristic geminate architecture with single-strand DNA bound to each coat protein (CP). The CP–CP and DNA–CP interactions, arranged in a CP–DNA–CP pattern at the interface, were partially observed. This suggests the genomic DNA plays an important role in forming a stable interface during assembly of the geminate particle.
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spelling pubmed-64809542019-04-29 Cryo-EM Structure of a Begomovirus Geminate Particle Xu, Xiongbiao Zhang, Qing Hong, Jian Li, Zhenghe Zhang, Xiaokang Zhou, Xueping Int J Mol Sci Article Tobacco curly shoot virus, a monopartite begomovirus associated with betasatellite, causes serious leaf curl diseases on tomato and tobacco in China. Using single-particle cryo-electron microscopy, we determined the structure of tobacco curly shoot virus (TbCSV) particle at 3.57 Å resolution and confirmed the characteristic geminate architecture with single-strand DNA bound to each coat protein (CP). The CP–CP and DNA–CP interactions, arranged in a CP–DNA–CP pattern at the interface, were partially observed. This suggests the genomic DNA plays an important role in forming a stable interface during assembly of the geminate particle. MDPI 2019-04-08 /pmc/articles/PMC6480954/ /pubmed/30965627 http://dx.doi.org/10.3390/ijms20071738 Text en © 2019 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 Article
Xu, Xiongbiao
Zhang, Qing
Hong, Jian
Li, Zhenghe
Zhang, Xiaokang
Zhou, Xueping
Cryo-EM Structure of a Begomovirus Geminate Particle
title Cryo-EM Structure of a Begomovirus Geminate Particle
title_full Cryo-EM Structure of a Begomovirus Geminate Particle
title_fullStr Cryo-EM Structure of a Begomovirus Geminate Particle
title_full_unstemmed Cryo-EM Structure of a Begomovirus Geminate Particle
title_short Cryo-EM Structure of a Begomovirus Geminate Particle
title_sort cryo-em structure of a begomovirus geminate particle
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6480954/
https://www.ncbi.nlm.nih.gov/pubmed/30965627
http://dx.doi.org/10.3390/ijms20071738
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