Cargando…
Unravelling the involvement of cilevirus p32 protein in the viral transport
Citrus leprosis (CL) is a severe disease that affects citrus orchards mainly in Latin America. It is caused by Brevipalpus-transmitted viruses from genera Cilevirus and Dichorhavirus. Currently, no reports have explored the movement machinery for the cilevirus. Here, we have performed a detailed fun...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7859179/ https://www.ncbi.nlm.nih.gov/pubmed/33536554 http://dx.doi.org/10.1038/s41598-021-82453-4 |
_version_ | 1783646672280092672 |
---|---|
author | Leastro, Mikhail Oliveira Freitas-Astúa, Juliana Kitajima, Elliot Watanabe Pallás, Vicente Sánchez-Navarro, Jesús A. |
author_facet | Leastro, Mikhail Oliveira Freitas-Astúa, Juliana Kitajima, Elliot Watanabe Pallás, Vicente Sánchez-Navarro, Jesús A. |
author_sort | Leastro, Mikhail Oliveira |
collection | PubMed |
description | Citrus leprosis (CL) is a severe disease that affects citrus orchards mainly in Latin America. It is caused by Brevipalpus-transmitted viruses from genera Cilevirus and Dichorhavirus. Currently, no reports have explored the movement machinery for the cilevirus. Here, we have performed a detailed functional study of the p32 movement protein (MP) of two cileviruses. Citrus leprosis-associated viruses are not able to move systemically in neither their natural nor experimental host plants. However, here we show that cilevirus MPs are able to allow the cell-to-cell and long-distance transport of movement-defective alfalfa mosaic virus (AMV). Several features related with the viral transport were explored, including: (i) the ability of cilevirus MPs to facilitate virus movement on a nucleocapsid assembly independent-manner; (ii) the generation of tubular structures from transient expression in protoplast; (iii) the capability of the N- and C- terminus of MP to interact with the cognate capsid protein (p29) and; (iv) the role of the C-terminus of p32 in the cell-to-cell and long-distance transport, tubule formation and the MP-plasmodesmata co-localization. The MP was able to direct the p29 to the plasmodesmata, whereby the C-terminus of MP is independently responsible to recruit the p29 to the cell periphery. Furthermore, we report that MP possess the capacity to enter the nucleolus and to bind to a major nucleolar protein, the fibrillarin. Based on our findings, we provide a model for the role of the p32 in the intra- and intercellular viral spread. |
format | Online Article Text |
id | pubmed-7859179 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-78591792021-02-04 Unravelling the involvement of cilevirus p32 protein in the viral transport Leastro, Mikhail Oliveira Freitas-Astúa, Juliana Kitajima, Elliot Watanabe Pallás, Vicente Sánchez-Navarro, Jesús A. Sci Rep Article Citrus leprosis (CL) is a severe disease that affects citrus orchards mainly in Latin America. It is caused by Brevipalpus-transmitted viruses from genera Cilevirus and Dichorhavirus. Currently, no reports have explored the movement machinery for the cilevirus. Here, we have performed a detailed functional study of the p32 movement protein (MP) of two cileviruses. Citrus leprosis-associated viruses are not able to move systemically in neither their natural nor experimental host plants. However, here we show that cilevirus MPs are able to allow the cell-to-cell and long-distance transport of movement-defective alfalfa mosaic virus (AMV). Several features related with the viral transport were explored, including: (i) the ability of cilevirus MPs to facilitate virus movement on a nucleocapsid assembly independent-manner; (ii) the generation of tubular structures from transient expression in protoplast; (iii) the capability of the N- and C- terminus of MP to interact with the cognate capsid protein (p29) and; (iv) the role of the C-terminus of p32 in the cell-to-cell and long-distance transport, tubule formation and the MP-plasmodesmata co-localization. The MP was able to direct the p29 to the plasmodesmata, whereby the C-terminus of MP is independently responsible to recruit the p29 to the cell periphery. Furthermore, we report that MP possess the capacity to enter the nucleolus and to bind to a major nucleolar protein, the fibrillarin. Based on our findings, we provide a model for the role of the p32 in the intra- and intercellular viral spread. Nature Publishing Group UK 2021-02-03 /pmc/articles/PMC7859179/ /pubmed/33536554 http://dx.doi.org/10.1038/s41598-021-82453-4 Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Leastro, Mikhail Oliveira Freitas-Astúa, Juliana Kitajima, Elliot Watanabe Pallás, Vicente Sánchez-Navarro, Jesús A. Unravelling the involvement of cilevirus p32 protein in the viral transport |
title | Unravelling the involvement of cilevirus p32 protein in the viral transport |
title_full | Unravelling the involvement of cilevirus p32 protein in the viral transport |
title_fullStr | Unravelling the involvement of cilevirus p32 protein in the viral transport |
title_full_unstemmed | Unravelling the involvement of cilevirus p32 protein in the viral transport |
title_short | Unravelling the involvement of cilevirus p32 protein in the viral transport |
title_sort | unravelling the involvement of cilevirus p32 protein in the viral transport |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7859179/ https://www.ncbi.nlm.nih.gov/pubmed/33536554 http://dx.doi.org/10.1038/s41598-021-82453-4 |
work_keys_str_mv | AT leastromikhailoliveira unravellingtheinvolvementofcilevirusp32proteinintheviraltransport AT freitasastuajuliana unravellingtheinvolvementofcilevirusp32proteinintheviraltransport AT kitajimaelliotwatanabe unravellingtheinvolvementofcilevirusp32proteinintheviraltransport AT pallasvicente unravellingtheinvolvementofcilevirusp32proteinintheviraltransport AT sancheznavarrojesusa unravellingtheinvolvementofcilevirusp32proteinintheviraltransport |