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Quantitative Proteomic Analysis Uncovers the Mediation of Endoplasmic Reticulum Stress-Induced Autophagy in DHAV-1-Infected DEF Cells

Autophagy is a tightly regulated catabolic process and is activated in cells in response to stress signals. Despite extensive study, the interplay between duck hepatitis A virus type 1 (DHAV-1) and the autophagy of host cells is not clear. In this study, we applied proteomics analysis to investigate...

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Autores principales: Lan, Jingjing, Zhang, Ruihua, Yu, Honglei, Wang, Jingyu, Xue, Wenxiang, Chen, Junhao, Lin, Shaoli, Wang, Yu, Xie, Zhijing, Jiang, Shijin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6940786/
https://www.ncbi.nlm.nih.gov/pubmed/31817666
http://dx.doi.org/10.3390/ijms20246160
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author Lan, Jingjing
Zhang, Ruihua
Yu, Honglei
Wang, Jingyu
Xue, Wenxiang
Chen, Junhao
Lin, Shaoli
Wang, Yu
Xie, Zhijing
Jiang, Shijin
author_facet Lan, Jingjing
Zhang, Ruihua
Yu, Honglei
Wang, Jingyu
Xue, Wenxiang
Chen, Junhao
Lin, Shaoli
Wang, Yu
Xie, Zhijing
Jiang, Shijin
author_sort Lan, Jingjing
collection PubMed
description Autophagy is a tightly regulated catabolic process and is activated in cells in response to stress signals. Despite extensive study, the interplay between duck hepatitis A virus type 1 (DHAV-1) and the autophagy of host cells is not clear. In this study, we applied proteomics analysis to investigate the interaction mechanism between DHAV-1 and duck embryo fibroblast (DEF) cells. In total, 507 differentially expressed proteins (DEPs) were identified, with 171 upregulated proteins and 336 downregulated proteins. The protein expression level of heat shock proteins (Hsps) and their response to stimulus proteins and zinc finger proteins (ZFPs) were significantly increased while the same aspects of ribosome proteins declined. Bioinformatics analysis indicated that DEPs were mainly involved in the “response to stimulus”, the “defense response to virus”, and the “phagosome pathway”. Furthermore, Western blot results showed that the conversion of microtubule-associated protein 1 light chain 3-I (LC3-I) to the lipidation form of LC3-II increased, and the conversion rate decreased when DEF cells were processed with 4-phenylbutyrate (4-PBA). These findings indicated that DHAV-1 infection could cause endoplasmic reticulum (ER) stress-induced autophagy in DEF cells, and that ER stress was an important regulatory factor in the activation of autophagy. Our data provide a new clue regarding the host cell response to DHAV-1 and identify proteins involved in the DHAV-1 infection process or the ER stress-induced autophagy process.
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spelling pubmed-69407862020-01-09 Quantitative Proteomic Analysis Uncovers the Mediation of Endoplasmic Reticulum Stress-Induced Autophagy in DHAV-1-Infected DEF Cells Lan, Jingjing Zhang, Ruihua Yu, Honglei Wang, Jingyu Xue, Wenxiang Chen, Junhao Lin, Shaoli Wang, Yu Xie, Zhijing Jiang, Shijin Int J Mol Sci Article Autophagy is a tightly regulated catabolic process and is activated in cells in response to stress signals. Despite extensive study, the interplay between duck hepatitis A virus type 1 (DHAV-1) and the autophagy of host cells is not clear. In this study, we applied proteomics analysis to investigate the interaction mechanism between DHAV-1 and duck embryo fibroblast (DEF) cells. In total, 507 differentially expressed proteins (DEPs) were identified, with 171 upregulated proteins and 336 downregulated proteins. The protein expression level of heat shock proteins (Hsps) and their response to stimulus proteins and zinc finger proteins (ZFPs) were significantly increased while the same aspects of ribosome proteins declined. Bioinformatics analysis indicated that DEPs were mainly involved in the “response to stimulus”, the “defense response to virus”, and the “phagosome pathway”. Furthermore, Western blot results showed that the conversion of microtubule-associated protein 1 light chain 3-I (LC3-I) to the lipidation form of LC3-II increased, and the conversion rate decreased when DEF cells were processed with 4-phenylbutyrate (4-PBA). These findings indicated that DHAV-1 infection could cause endoplasmic reticulum (ER) stress-induced autophagy in DEF cells, and that ER stress was an important regulatory factor in the activation of autophagy. Our data provide a new clue regarding the host cell response to DHAV-1 and identify proteins involved in the DHAV-1 infection process or the ER stress-induced autophagy process. MDPI 2019-12-06 /pmc/articles/PMC6940786/ /pubmed/31817666 http://dx.doi.org/10.3390/ijms20246160 Text en © 2019 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Lan, Jingjing
Zhang, Ruihua
Yu, Honglei
Wang, Jingyu
Xue, Wenxiang
Chen, Junhao
Lin, Shaoli
Wang, Yu
Xie, Zhijing
Jiang, Shijin
Quantitative Proteomic Analysis Uncovers the Mediation of Endoplasmic Reticulum Stress-Induced Autophagy in DHAV-1-Infected DEF Cells
title Quantitative Proteomic Analysis Uncovers the Mediation of Endoplasmic Reticulum Stress-Induced Autophagy in DHAV-1-Infected DEF Cells
title_full Quantitative Proteomic Analysis Uncovers the Mediation of Endoplasmic Reticulum Stress-Induced Autophagy in DHAV-1-Infected DEF Cells
title_fullStr Quantitative Proteomic Analysis Uncovers the Mediation of Endoplasmic Reticulum Stress-Induced Autophagy in DHAV-1-Infected DEF Cells
title_full_unstemmed Quantitative Proteomic Analysis Uncovers the Mediation of Endoplasmic Reticulum Stress-Induced Autophagy in DHAV-1-Infected DEF Cells
title_short Quantitative Proteomic Analysis Uncovers the Mediation of Endoplasmic Reticulum Stress-Induced Autophagy in DHAV-1-Infected DEF Cells
title_sort quantitative proteomic analysis uncovers the mediation of endoplasmic reticulum stress-induced autophagy in dhav-1-infected def cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6940786/
https://www.ncbi.nlm.nih.gov/pubmed/31817666
http://dx.doi.org/10.3390/ijms20246160
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