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A conserved motif in three viral movement proteins from different genera is required for host factor recruitment and cell-to-cell movement

Due to their minimal genomes, plant viruses are forced to hijack specific cellular pathways to ensure host colonization, a condition that most frequently involves physical interaction between viral and host proteins. Among putative viral interactors are the movement proteins, responsible for plasmod...

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Autores principales: Navarro, José A., Serra-Soriano, Marta, Corachán-Valencia, Lorena, Pallás, Vicente
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7075923/
https://www.ncbi.nlm.nih.gov/pubmed/32179855
http://dx.doi.org/10.1038/s41598-020-61741-5
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author Navarro, José A.
Serra-Soriano, Marta
Corachán-Valencia, Lorena
Pallás, Vicente
author_facet Navarro, José A.
Serra-Soriano, Marta
Corachán-Valencia, Lorena
Pallás, Vicente
author_sort Navarro, José A.
collection PubMed
description Due to their minimal genomes, plant viruses are forced to hijack specific cellular pathways to ensure host colonization, a condition that most frequently involves physical interaction between viral and host proteins. Among putative viral interactors are the movement proteins, responsible for plasmodesma gating and genome binding during viral transport. Two of them, DGBp1 and DGBp2, are required for alpha-, beta- and gammacarmovirus cell-to-cell movement, but the number of DGBp-host interactors identified at present is limited. By using two different approaches, yeast two-hybrid and bimolecular fluorescence complementation assays, we found three Arabidopsis factors, eIF3g1, RPP3A and WRKY36, interacting with DGBp1s from each genus mentioned above. eIF3g1 and RPP3A are mainly involved in protein translation initiation and elongation phases, respectively, while WRKY36 belongs to WRKY transcription factor family, important regulators of many defence responses. These host proteins are not expected to be associated with viral movement, but knocking out WRKY36 or silencing either RPP3A or eIF3g1 negatively affected Arabidopsis infection by Turnip crinkle virus. A highly conserved FNF motif at DGBp1 C-terminus was required for protein-protein interaction and cell-to-cell movement, suggesting an important biological role.
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spelling pubmed-70759232020-03-23 A conserved motif in three viral movement proteins from different genera is required for host factor recruitment and cell-to-cell movement Navarro, José A. Serra-Soriano, Marta Corachán-Valencia, Lorena Pallás, Vicente Sci Rep Article Due to their minimal genomes, plant viruses are forced to hijack specific cellular pathways to ensure host colonization, a condition that most frequently involves physical interaction between viral and host proteins. Among putative viral interactors are the movement proteins, responsible for plasmodesma gating and genome binding during viral transport. Two of them, DGBp1 and DGBp2, are required for alpha-, beta- and gammacarmovirus cell-to-cell movement, but the number of DGBp-host interactors identified at present is limited. By using two different approaches, yeast two-hybrid and bimolecular fluorescence complementation assays, we found three Arabidopsis factors, eIF3g1, RPP3A and WRKY36, interacting with DGBp1s from each genus mentioned above. eIF3g1 and RPP3A are mainly involved in protein translation initiation and elongation phases, respectively, while WRKY36 belongs to WRKY transcription factor family, important regulators of many defence responses. These host proteins are not expected to be associated with viral movement, but knocking out WRKY36 or silencing either RPP3A or eIF3g1 negatively affected Arabidopsis infection by Turnip crinkle virus. A highly conserved FNF motif at DGBp1 C-terminus was required for protein-protein interaction and cell-to-cell movement, suggesting an important biological role. Nature Publishing Group UK 2020-03-16 /pmc/articles/PMC7075923/ /pubmed/32179855 http://dx.doi.org/10.1038/s41598-020-61741-5 Text en © The Author(s) 2020 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Navarro, José A.
Serra-Soriano, Marta
Corachán-Valencia, Lorena
Pallás, Vicente
A conserved motif in three viral movement proteins from different genera is required for host factor recruitment and cell-to-cell movement
title A conserved motif in three viral movement proteins from different genera is required for host factor recruitment and cell-to-cell movement
title_full A conserved motif in three viral movement proteins from different genera is required for host factor recruitment and cell-to-cell movement
title_fullStr A conserved motif in three viral movement proteins from different genera is required for host factor recruitment and cell-to-cell movement
title_full_unstemmed A conserved motif in three viral movement proteins from different genera is required for host factor recruitment and cell-to-cell movement
title_short A conserved motif in three viral movement proteins from different genera is required for host factor recruitment and cell-to-cell movement
title_sort conserved motif in three viral movement proteins from different genera is required for host factor recruitment and cell-to-cell movement
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7075923/
https://www.ncbi.nlm.nih.gov/pubmed/32179855
http://dx.doi.org/10.1038/s41598-020-61741-5
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