Multiple aromatic amino acids are involved in potyvirus movement by forming π-stackings to maintain coat protein accumulation
Abstract Coat protein (CP) is required for potyviruses to move and establish a systemic infection in plants. π-stackings formed by aromatic residues play critical roles in maintaining protein stability and functions. As we know, many aromatic residues located in the core region of potyvirus CPs are...
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doaj-0afc10e2d83b45878dca7fb43e05bf4f2021-05-23T11:43:53ZengBMCPhytopathology Research2524-41672021-05-013111310.1186/s42483-021-00088-9Multiple aromatic amino acids are involved in potyvirus movement by forming π-stackings to maintain coat protein accumulationZhi-Yong Yan0Xiao-Jie Xu1Le Fang2Chao Geng3Yan-Ping Tian4Xiang-Dong Li5Laboratory of Plant Virology, College of Plant Protection, Shandong Agricultural UniversityLaboratory of Plant Virology, College of Plant Protection, Shandong Agricultural UniversityLaboratory of Plant Virology, College of Plant Protection, Shandong Agricultural UniversityLaboratory of Plant Virology, College of Plant Protection, Shandong Agricultural UniversityLaboratory of Plant Virology, College of Plant Protection, Shandong Agricultural UniversityLaboratory of Plant Virology, College of Plant Protection, Shandong Agricultural UniversityAbstract Coat protein (CP) is required for potyviruses to move and establish a systemic infection in plants. π-stackings formed by aromatic residues play critical roles in maintaining protein stability and functions. As we know, many aromatic residues located in the core region of potyvirus CPs are conserved. However, their roles in potyvirus infection remain largely unknown. Here, through analysis of the three-dimensional model of the tobacco vein banding mosaic virus (TVBMV; genus Potyvirus) CP, 16 aromatic residues were predicated to form π-stackings. The results of transient expression experiments demonstrated that deletion of any of these 16 aromatic residues reduced CP accumulation. Infectivity assays showed that deletion of any of these aromatic residues in the TVBMV infectious clone abolished cell-to-cell movement and reduced replication of the virus. Substitution of Y105 and Y147 individually with non-aromatic residues alanine or glycine reduced CP accumulation, virus replication, and abolished the ability of TVBMV to move intercellularly, while substitution of these two residues individually with aromatic residues phenylalanine or tryptophan, had no or little effect on CP accumulation and TVBMV systemic movement and replication. Similar results were obtained from the CP mutants of watermelon mosaic virus (WMV, genus Potyvirus). Taken together, our results demonstrate that multiple aromatic residues in CP are involved in potyvirus movement by forming π-stackings to maintain CP accumulation.https://doi.org/10.1186/s42483-021-00088-9Coat proteinMovementπ-stackingPotyvirusStabilityTobacco vein banding mosaic virus |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Zhi-Yong Yan Xiao-Jie Xu Le Fang Chao Geng Yan-Ping Tian Xiang-Dong Li |
spellingShingle |
Zhi-Yong Yan Xiao-Jie Xu Le Fang Chao Geng Yan-Ping Tian Xiang-Dong Li Multiple aromatic amino acids are involved in potyvirus movement by forming π-stackings to maintain coat protein accumulation Phytopathology Research Coat protein Movement π-stacking Potyvirus Stability Tobacco vein banding mosaic virus |
author_facet |
Zhi-Yong Yan Xiao-Jie Xu Le Fang Chao Geng Yan-Ping Tian Xiang-Dong Li |
author_sort |
Zhi-Yong Yan |
title |
Multiple aromatic amino acids are involved in potyvirus movement by forming π-stackings to maintain coat protein accumulation |
title_short |
Multiple aromatic amino acids are involved in potyvirus movement by forming π-stackings to maintain coat protein accumulation |
title_full |
Multiple aromatic amino acids are involved in potyvirus movement by forming π-stackings to maintain coat protein accumulation |
title_fullStr |
Multiple aromatic amino acids are involved in potyvirus movement by forming π-stackings to maintain coat protein accumulation |
title_full_unstemmed |
Multiple aromatic amino acids are involved in potyvirus movement by forming π-stackings to maintain coat protein accumulation |
title_sort |
multiple aromatic amino acids are involved in potyvirus movement by forming π-stackings to maintain coat protein accumulation |
publisher |
BMC |
series |
Phytopathology Research |
issn |
2524-4167 |
publishDate |
2021-05-01 |
description |
Abstract Coat protein (CP) is required for potyviruses to move and establish a systemic infection in plants. π-stackings formed by aromatic residues play critical roles in maintaining protein stability and functions. As we know, many aromatic residues located in the core region of potyvirus CPs are conserved. However, their roles in potyvirus infection remain largely unknown. Here, through analysis of the three-dimensional model of the tobacco vein banding mosaic virus (TVBMV; genus Potyvirus) CP, 16 aromatic residues were predicated to form π-stackings. The results of transient expression experiments demonstrated that deletion of any of these 16 aromatic residues reduced CP accumulation. Infectivity assays showed that deletion of any of these aromatic residues in the TVBMV infectious clone abolished cell-to-cell movement and reduced replication of the virus. Substitution of Y105 and Y147 individually with non-aromatic residues alanine or glycine reduced CP accumulation, virus replication, and abolished the ability of TVBMV to move intercellularly, while substitution of these two residues individually with aromatic residues phenylalanine or tryptophan, had no or little effect on CP accumulation and TVBMV systemic movement and replication. Similar results were obtained from the CP mutants of watermelon mosaic virus (WMV, genus Potyvirus). Taken together, our results demonstrate that multiple aromatic residues in CP are involved in potyvirus movement by forming π-stackings to maintain CP accumulation. |
topic |
Coat protein Movement π-stacking Potyvirus Stability Tobacco vein banding mosaic virus |
url |
https://doi.org/10.1186/s42483-021-00088-9 |
work_keys_str_mv |
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