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Exploring the Multifunctional Roles of Odontoglossum Ringspot Virus P126 in Facilitating Cymbidium Mosaic Virus Cell-to-Cell Movement during Mixed Infection

Synergistic interactions among viruses, hosts and/or transmission vectors during mixed infection can alter viral titers, symptom severity or host range. Viral suppressors of RNA silencing (VSRs) are considered one of such factors contributing to synergistic responses. Odontoglossum ringspot virus (O...

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Autores principales: Lee, Shu-Chuan, Pai, Hsuan, Huang, Ying-Wen, He, Meng-Hsun, Song, Yun-Lin, Kuo, Song-Yi, Chang, Wen-Chi, Hsu, Yau-Heiu, Lin, Na-Sheng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8402721/
https://www.ncbi.nlm.nih.gov/pubmed/34452417
http://dx.doi.org/10.3390/v13081552
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author Lee, Shu-Chuan
Pai, Hsuan
Huang, Ying-Wen
He, Meng-Hsun
Song, Yun-Lin
Kuo, Song-Yi
Chang, Wen-Chi
Hsu, Yau-Heiu
Lin, Na-Sheng
author_facet Lee, Shu-Chuan
Pai, Hsuan
Huang, Ying-Wen
He, Meng-Hsun
Song, Yun-Lin
Kuo, Song-Yi
Chang, Wen-Chi
Hsu, Yau-Heiu
Lin, Na-Sheng
author_sort Lee, Shu-Chuan
collection PubMed
description Synergistic interactions among viruses, hosts and/or transmission vectors during mixed infection can alter viral titers, symptom severity or host range. Viral suppressors of RNA silencing (VSRs) are considered one of such factors contributing to synergistic responses. Odontoglossum ringspot virus (ORSV) and cymbidium mosaic virus (CymMV), which are two of the most significant orchid viruses, exhibit synergistic symptom intensification in Phalaenopsis orchids with unilaterally enhanced CymMV movement by ORSV. In order to reveal the underlying mechanisms, we generated infectious cDNA clones of ORSV and CymMV isolated from Phalaenopsis that exerted similar unilateral synergism in both Phalaenopsis orchid and Nicotiana benthamiana. Moreover, we show that the ORSV replicase P126 is a VSR. Mutagenesis analysis revealed that mutation of the methionine in the carboxyl terminus of ORSV P126 abolished ORSV replication even though some P126 mutants preserved VSR activity, indicating that the VSR function of P126 alone is not sufficient for viral replication. Thus, P126 functions in both ORSV replication and as a VSR. Furthermore, P126 expression enhanced cell-to-cell movement and viral titers of CymMV in infected Phalaenopsis flowers and N. benthamiana leaves. Taking together, both the VSR and protein function of P126 might be prerequisites for unilaterally enhancing CymMV cell-to-cell movement by ORSV.
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spelling pubmed-84027212021-08-29 Exploring the Multifunctional Roles of Odontoglossum Ringspot Virus P126 in Facilitating Cymbidium Mosaic Virus Cell-to-Cell Movement during Mixed Infection Lee, Shu-Chuan Pai, Hsuan Huang, Ying-Wen He, Meng-Hsun Song, Yun-Lin Kuo, Song-Yi Chang, Wen-Chi Hsu, Yau-Heiu Lin, Na-Sheng Viruses Article Synergistic interactions among viruses, hosts and/or transmission vectors during mixed infection can alter viral titers, symptom severity or host range. Viral suppressors of RNA silencing (VSRs) are considered one of such factors contributing to synergistic responses. Odontoglossum ringspot virus (ORSV) and cymbidium mosaic virus (CymMV), which are two of the most significant orchid viruses, exhibit synergistic symptom intensification in Phalaenopsis orchids with unilaterally enhanced CymMV movement by ORSV. In order to reveal the underlying mechanisms, we generated infectious cDNA clones of ORSV and CymMV isolated from Phalaenopsis that exerted similar unilateral synergism in both Phalaenopsis orchid and Nicotiana benthamiana. Moreover, we show that the ORSV replicase P126 is a VSR. Mutagenesis analysis revealed that mutation of the methionine in the carboxyl terminus of ORSV P126 abolished ORSV replication even though some P126 mutants preserved VSR activity, indicating that the VSR function of P126 alone is not sufficient for viral replication. Thus, P126 functions in both ORSV replication and as a VSR. Furthermore, P126 expression enhanced cell-to-cell movement and viral titers of CymMV in infected Phalaenopsis flowers and N. benthamiana leaves. Taking together, both the VSR and protein function of P126 might be prerequisites for unilaterally enhancing CymMV cell-to-cell movement by ORSV. MDPI 2021-08-06 /pmc/articles/PMC8402721/ /pubmed/34452417 http://dx.doi.org/10.3390/v13081552 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Lee, Shu-Chuan
Pai, Hsuan
Huang, Ying-Wen
He, Meng-Hsun
Song, Yun-Lin
Kuo, Song-Yi
Chang, Wen-Chi
Hsu, Yau-Heiu
Lin, Na-Sheng
Exploring the Multifunctional Roles of Odontoglossum Ringspot Virus P126 in Facilitating Cymbidium Mosaic Virus Cell-to-Cell Movement during Mixed Infection
title Exploring the Multifunctional Roles of Odontoglossum Ringspot Virus P126 in Facilitating Cymbidium Mosaic Virus Cell-to-Cell Movement during Mixed Infection
title_full Exploring the Multifunctional Roles of Odontoglossum Ringspot Virus P126 in Facilitating Cymbidium Mosaic Virus Cell-to-Cell Movement during Mixed Infection
title_fullStr Exploring the Multifunctional Roles of Odontoglossum Ringspot Virus P126 in Facilitating Cymbidium Mosaic Virus Cell-to-Cell Movement during Mixed Infection
title_full_unstemmed Exploring the Multifunctional Roles of Odontoglossum Ringspot Virus P126 in Facilitating Cymbidium Mosaic Virus Cell-to-Cell Movement during Mixed Infection
title_short Exploring the Multifunctional Roles of Odontoglossum Ringspot Virus P126 in Facilitating Cymbidium Mosaic Virus Cell-to-Cell Movement during Mixed Infection
title_sort exploring the multifunctional roles of odontoglossum ringspot virus p126 in facilitating cymbidium mosaic virus cell-to-cell movement during mixed infection
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8402721/
https://www.ncbi.nlm.nih.gov/pubmed/34452417
http://dx.doi.org/10.3390/v13081552
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