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Altered Proteomic Profile of Exosomes Secreted from Vero Cells Infected with Porcine Epidemic Diarrhea Virus
Porcine epidemic diarrhea virus (PEDV) infection causes severe diarrhea in pigs and can be fatal in newborn piglets. Exosomes are extracellular vesicles secreted by cells that transfer biologically active proteins, lipids, and RNA to neighboring or distant cells. Herein, the morphology, particle siz...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10459195/ https://www.ncbi.nlm.nih.gov/pubmed/37631983 http://dx.doi.org/10.3390/v15081640 |
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author | Shen, Xuehuai Yin, Lei Xu, Shuangshuang Wang, Jieru Yin, Dongdong Zhao, Ruihong Pan, Xiaocheng Dai, Yin Hou, Hongyan Zhou, Xueli Hu, Xiaomiao |
author_facet | Shen, Xuehuai Yin, Lei Xu, Shuangshuang Wang, Jieru Yin, Dongdong Zhao, Ruihong Pan, Xiaocheng Dai, Yin Hou, Hongyan Zhou, Xueli Hu, Xiaomiao |
author_sort | Shen, Xuehuai |
collection | PubMed |
description | Porcine epidemic diarrhea virus (PEDV) infection causes severe diarrhea in pigs and can be fatal in newborn piglets. Exosomes are extracellular vesicles secreted by cells that transfer biologically active proteins, lipids, and RNA to neighboring or distant cells. Herein, the morphology, particle size, and secretion of exosomes derived from a control and PEDV-infected group are examined, followed by a proteomic analysis of the exosomes. The results show that the exosomes secreted from the Vero cells had a typical cup–shaped structure. The average particle size of the exosomes from the PEDV-infected group was 112.4 nm, whereas that from the control group was 150.8 nm. The exosome density analysis and characteristic protein determination revealed that the content of exosomes in the PEDV-infected group was significantly higher than that in the control group. The quantitative proteomics assays revealed 544 differentially expressed proteins (DEPs) in the PEDV-infected group’s exosomes compared with those in the controls, with 236 upregulated and 308 downregulated proteins. The DEPs were closely associated with cellular regulatory pathways, such as the phosphatidylinositol–4,5–bisphosphate 3–kinase (PI3K)–protein kinase B (Akt) signaling pathway, extracellular matrix–receptor interaction, focal adhesion, and cytoskeletal regulation. These findings provide the basis for further investigation of the pathogenic mechanisms of PEDV and the discovery of novel antiviral targets. |
format | Online Article Text |
id | pubmed-10459195 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-104591952023-08-27 Altered Proteomic Profile of Exosomes Secreted from Vero Cells Infected with Porcine Epidemic Diarrhea Virus Shen, Xuehuai Yin, Lei Xu, Shuangshuang Wang, Jieru Yin, Dongdong Zhao, Ruihong Pan, Xiaocheng Dai, Yin Hou, Hongyan Zhou, Xueli Hu, Xiaomiao Viruses Article Porcine epidemic diarrhea virus (PEDV) infection causes severe diarrhea in pigs and can be fatal in newborn piglets. Exosomes are extracellular vesicles secreted by cells that transfer biologically active proteins, lipids, and RNA to neighboring or distant cells. Herein, the morphology, particle size, and secretion of exosomes derived from a control and PEDV-infected group are examined, followed by a proteomic analysis of the exosomes. The results show that the exosomes secreted from the Vero cells had a typical cup–shaped structure. The average particle size of the exosomes from the PEDV-infected group was 112.4 nm, whereas that from the control group was 150.8 nm. The exosome density analysis and characteristic protein determination revealed that the content of exosomes in the PEDV-infected group was significantly higher than that in the control group. The quantitative proteomics assays revealed 544 differentially expressed proteins (DEPs) in the PEDV-infected group’s exosomes compared with those in the controls, with 236 upregulated and 308 downregulated proteins. The DEPs were closely associated with cellular regulatory pathways, such as the phosphatidylinositol–4,5–bisphosphate 3–kinase (PI3K)–protein kinase B (Akt) signaling pathway, extracellular matrix–receptor interaction, focal adhesion, and cytoskeletal regulation. These findings provide the basis for further investigation of the pathogenic mechanisms of PEDV and the discovery of novel antiviral targets. MDPI 2023-07-27 /pmc/articles/PMC10459195/ /pubmed/37631983 http://dx.doi.org/10.3390/v15081640 Text en © 2023 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 Shen, Xuehuai Yin, Lei Xu, Shuangshuang Wang, Jieru Yin, Dongdong Zhao, Ruihong Pan, Xiaocheng Dai, Yin Hou, Hongyan Zhou, Xueli Hu, Xiaomiao Altered Proteomic Profile of Exosomes Secreted from Vero Cells Infected with Porcine Epidemic Diarrhea Virus |
title | Altered Proteomic Profile of Exosomes Secreted from Vero Cells Infected with Porcine Epidemic Diarrhea Virus |
title_full | Altered Proteomic Profile of Exosomes Secreted from Vero Cells Infected with Porcine Epidemic Diarrhea Virus |
title_fullStr | Altered Proteomic Profile of Exosomes Secreted from Vero Cells Infected with Porcine Epidemic Diarrhea Virus |
title_full_unstemmed | Altered Proteomic Profile of Exosomes Secreted from Vero Cells Infected with Porcine Epidemic Diarrhea Virus |
title_short | Altered Proteomic Profile of Exosomes Secreted from Vero Cells Infected with Porcine Epidemic Diarrhea Virus |
title_sort | altered proteomic profile of exosomes secreted from vero cells infected with porcine epidemic diarrhea virus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10459195/ https://www.ncbi.nlm.nih.gov/pubmed/37631983 http://dx.doi.org/10.3390/v15081640 |
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