Single amino acid in V2 encoded by TYLCV is responsible for its self-interaction, aggregates and pathogenicity

Abstract The V2 protein encoded by Begomovirus is essential for virus infection and is involved in multiple functions, such as virus movement and suppression of the host defence response. In this study, we reported that V2 encoded by the Tomato yellow leaf curl virus (TYLCV), which is one of the mos...

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Autores principales:	Wenhao Zhao, Yinghua Ji, Shuhua Wu, Xiaofang Ma, Shuo Li, Feng Sun, Zhaobang Cheng, Yijun Zhou, Yongjian Fan
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/bf932a3c885d4a64bfe10aa60344e785
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spelling	oai:doaj.org-article:bf932a3c885d4a64bfe10aa60344e7852021-12-02T15:08:58ZSingle amino acid in V2 encoded by TYLCV is responsible for its self-interaction, aggregates and pathogenicity10.1038/s41598-018-21446-22045-2322https://doaj.org/article/bf932a3c885d4a64bfe10aa60344e7852018-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-21446-2https://doaj.org/toc/2045-2322Abstract The V2 protein encoded by Begomovirus is essential for virus infection and is involved in multiple functions, such as virus movement and suppression of the host defence response. In this study, we reported that V2 encoded by the Tomato yellow leaf curl virus (TYLCV), which is one of the most devastating tomato-infecting begomoviruses, could interact with itself and a S71A mutation of V2 (V2S71A) abolished its self-interaction. Fluorescence results showed that V2 localized primarily in the cytoplasm and around the nucleus. Site-directed mutagenesis V2S71A had the similar subcellular localization, but V2S71A formed fewer large aggregates in the cytoplasm compared to wild-type V2, whereas the level of aggregates came to a similar after treatment with MG132, which indicates that the S71A mutation might affect 26S proteasome-mediated degradation of V2 aggregates. Meanwhile, heterologous expression of V2S71A from a Potato virus X vector induced mild symptoms compared to wild-type V2, delay of virus infection associated with mild symptoms was observed in plants inoculated with TYLCV-S71A, which indicates that the amino acid on position 71 is also involved in the pathogenicity of V2. To the best of our knowledge, this report is the first to state that the S71A mutation of V2 encoded by TYLCV affects the self-interaction, aggregate formation and pathogenicity of V2.Wenhao ZhaoYinghua JiShuhua WuXiaofang MaShuo LiFeng SunZhaobang ChengYijun ZhouYongjian FanNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Wenhao Zhao Yinghua Ji Shuhua Wu Xiaofang Ma Shuo Li Feng Sun Zhaobang Cheng Yijun Zhou Yongjian Fan Single amino acid in V2 encoded by TYLCV is responsible for its self-interaction, aggregates and pathogenicity
description	Abstract The V2 protein encoded by Begomovirus is essential for virus infection and is involved in multiple functions, such as virus movement and suppression of the host defence response. In this study, we reported that V2 encoded by the Tomato yellow leaf curl virus (TYLCV), which is one of the most devastating tomato-infecting begomoviruses, could interact with itself and a S71A mutation of V2 (V2S71A) abolished its self-interaction. Fluorescence results showed that V2 localized primarily in the cytoplasm and around the nucleus. Site-directed mutagenesis V2S71A had the similar subcellular localization, but V2S71A formed fewer large aggregates in the cytoplasm compared to wild-type V2, whereas the level of aggregates came to a similar after treatment with MG132, which indicates that the S71A mutation might affect 26S proteasome-mediated degradation of V2 aggregates. Meanwhile, heterologous expression of V2S71A from a Potato virus X vector induced mild symptoms compared to wild-type V2, delay of virus infection associated with mild symptoms was observed in plants inoculated with TYLCV-S71A, which indicates that the amino acid on position 71 is also involved in the pathogenicity of V2. To the best of our knowledge, this report is the first to state that the S71A mutation of V2 encoded by TYLCV affects the self-interaction, aggregate formation and pathogenicity of V2.
format	article
author	Wenhao Zhao Yinghua Ji Shuhua Wu Xiaofang Ma Shuo Li Feng Sun Zhaobang Cheng Yijun Zhou Yongjian Fan
author_facet	Wenhao Zhao Yinghua Ji Shuhua Wu Xiaofang Ma Shuo Li Feng Sun Zhaobang Cheng Yijun Zhou Yongjian Fan
author_sort	Wenhao Zhao
title	Single amino acid in V2 encoded by TYLCV is responsible for its self-interaction, aggregates and pathogenicity
title_short	Single amino acid in V2 encoded by TYLCV is responsible for its self-interaction, aggregates and pathogenicity
title_full	Single amino acid in V2 encoded by TYLCV is responsible for its self-interaction, aggregates and pathogenicity
title_fullStr	Single amino acid in V2 encoded by TYLCV is responsible for its self-interaction, aggregates and pathogenicity
title_full_unstemmed	Single amino acid in V2 encoded by TYLCV is responsible for its self-interaction, aggregates and pathogenicity
title_sort	single amino acid in v2 encoded by tylcv is responsible for its self-interaction, aggregates and pathogenicity
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/bf932a3c885d4a64bfe10aa60344e785
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Single amino acid in V2 encoded by TYLCV is responsible for its self-interaction, aggregates and pathogenicity

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