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Main Authors: Zeng, Zishan, Lin, Nanxin, Lu, Tao, Xu, Jian, Zhang, Zheng, Wang, Fang, Wang, Jinzi
Format: Artículo científico
Language:en
Published: Biology 2025
Online Access:https://pubmed.ncbi.nlm.nih.gov/41007270/
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author Zeng, Zishan
Lin, Nanxin
Lu, Tao
Xu, Jian
Zhang, Zheng
Wang, Fang
Wang, Jinzi
author_facet Zeng, Zishan
Lin, Nanxin
Lu, Tao
Xu, Jian
Zhang, Zheng
Wang, Fang
Wang, Jinzi
Zeng, Zishan
Lin, Nanxin
Lu, Tao
Xu, Jian
Zhang, Zheng
Wang, Fang
Wang, Jinzi
collection PubMed - marine biology
contents Evaluation of Hypovirus Infection on the Vesicular Protein Expression Pattern of by TMT-Based Proteomics Analysis. Zeng, Zishan Lin, Nanxin Lu, Tao Xu, Jian Zhang, Zheng Wang, Fang Wang, Jinzi Hypovirus infection is known to reduce the pathogenicity of , the causative agent of chestnut blight. Isoforms derived from a viral protein p48 have been discovered in host mitochondria and vesicles, which may contribute to virulence attenuation, as reported in earlier work using two-dimensional electrophoresis (2-DE). In this study, a total of 1739 fungal proteins were identified in fungal vesicles through Tandem Mass Tag (TMT)-based quantitative proteomics. The infection of CHV1-EP713 was associated with 75 up-regulated and 201 down-regulated proteins, predominantly involved in vesicular transport process and related cellular functions, including protein folding, membrane fusion, retrograde transport, autophagy, and ER stress responses. The down-regulation of calnexin, COPI, ArfGAP, importin-β, and Atg8 is consistent with impairments in protein folding, retrograde transport, and autophagy. Meanwhile, the up-regulation of clathrin, dynamin, Vps10p, HSP70, and t-SNAREs indicated enhanced trafficking to vacuoles and increased stress response activity. Overall, our findings indicate that hypoviral infection is associated with extensive alterations in the vesicular transport system of , likely mediated through changes in the abundance of multiple key protein regulators. These alterations may underlie attenuation of virulence by impacting crucial cellular processes.
format Artículo científico
id pubmed_41007270
institution PubMed
language en
publishDate 2025
publisher Biology
record_format pubmed
spellingShingle Evaluation of Hypovirus Infection on the Vesicular Protein Expression Pattern of by TMT-Based Proteomics Analysis.
Zeng, Zishan
Lin, Nanxin
Lu, Tao
Xu, Jian
Zhang, Zheng
Wang, Fang
Wang, Jinzi
Evaluation of Hypovirus Infection on the Vesicular Protein Expression Pattern of by TMT-Based Proteomics Analysis. Zeng, Zishan Lin, Nanxin Lu, Tao Xu, Jian Zhang, Zheng Wang, Fang Wang, Jinzi Hypovirus infection is known to reduce the pathogenicity of , the causative agent of chestnut blight. Isoforms derived from a viral protein p48 have been discovered in host mitochondria and vesicles, which may contribute to virulence attenuation, as reported in earlier work using two-dimensional electrophoresis (2-DE). In this study, a total of 1739 fungal proteins were identified in fungal vesicles through Tandem Mass Tag (TMT)-based quantitative proteomics. The infection of CHV1-EP713 was associated with 75 up-regulated and 201 down-regulated proteins, predominantly involved in vesicular transport process and related cellular functions, including protein folding, membrane fusion, retrograde transport, autophagy, and ER stress responses. The down-regulation of calnexin, COPI, ArfGAP, importin-β, and Atg8 is consistent with impairments in protein folding, retrograde transport, and autophagy. Meanwhile, the up-regulation of clathrin, dynamin, Vps10p, HSP70, and t-SNAREs indicated enhanced trafficking to vacuoles and increased stress response activity. Overall, our findings indicate that hypoviral infection is associated with extensive alterations in the vesicular transport system of , likely mediated through changes in the abundance of multiple key protein regulators. These alterations may underlie attenuation of virulence by impacting crucial cellular processes.
title Evaluation of Hypovirus Infection on the Vesicular Protein Expression Pattern of by TMT-Based Proteomics Analysis.
url https://pubmed.ncbi.nlm.nih.gov/41007270/