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Degradation of Host Proteins and Apoptosis Induced by Foot-and-Mouth Disease Virus 3C Protease
Foot-and-mouth disease (FMD), induced by the foot-and-mouth disease virus (FMDV), is a highly contagious disease of cloven-hoofed animals. Previous studies have reported that FMDV 3C protease could degrade multiple host proteins; however, the degradation mechanism mediated by FMDV 3C is still unclea...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8707164/ https://www.ncbi.nlm.nih.gov/pubmed/34959521 http://dx.doi.org/10.3390/pathogens10121566 |
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author | Yi, Jiamin Peng, Jiangling Ren, Jingjing Zhu, Guoqiang Ru, Yi Tian, Hong Li, Dan Zheng, Haixue |
author_facet | Yi, Jiamin Peng, Jiangling Ren, Jingjing Zhu, Guoqiang Ru, Yi Tian, Hong Li, Dan Zheng, Haixue |
author_sort | Yi, Jiamin |
collection | PubMed |
description | Foot-and-mouth disease (FMD), induced by the foot-and-mouth disease virus (FMDV), is a highly contagious disease of cloven-hoofed animals. Previous studies have reported that FMDV 3C protease could degrade multiple host proteins; however, the degradation mechanism mediated by FMDV 3C is still unclear. Here, we found that transient expression of FMDV 3C degraded various molecules in NF-κB signaling in a dose-dependent manner, and the proteolytic activity of FMDV 3C is important for inducing degradation. Additionally, 3C-overexpression was associated with the induction of apoptosis. In this study, we showed that an apoptosis inhibitor CrmA abolished the ability of 3C to degrade molecules in NF-κB signaling. Further experiments using specific caspase inhibitors confirmed the irrelevance of caspase3, caspase8, and caspase9 activity for degradation induced by 3C. Altogether, these results suggest that FMDV 3C induces the widespread degradation of host proteins through its proteolytic activity and that the apoptosis pathway might be an important strategy to mediate this process. Further exploration of the relationship between apoptosis and degradation induced by 3C could provide novel insights into the pathogenic mechanisms of FMDV. |
format | Online Article Text |
id | pubmed-8707164 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-87071642021-12-25 Degradation of Host Proteins and Apoptosis Induced by Foot-and-Mouth Disease Virus 3C Protease Yi, Jiamin Peng, Jiangling Ren, Jingjing Zhu, Guoqiang Ru, Yi Tian, Hong Li, Dan Zheng, Haixue Pathogens Article Foot-and-mouth disease (FMD), induced by the foot-and-mouth disease virus (FMDV), is a highly contagious disease of cloven-hoofed animals. Previous studies have reported that FMDV 3C protease could degrade multiple host proteins; however, the degradation mechanism mediated by FMDV 3C is still unclear. Here, we found that transient expression of FMDV 3C degraded various molecules in NF-κB signaling in a dose-dependent manner, and the proteolytic activity of FMDV 3C is important for inducing degradation. Additionally, 3C-overexpression was associated with the induction of apoptosis. In this study, we showed that an apoptosis inhibitor CrmA abolished the ability of 3C to degrade molecules in NF-κB signaling. Further experiments using specific caspase inhibitors confirmed the irrelevance of caspase3, caspase8, and caspase9 activity for degradation induced by 3C. Altogether, these results suggest that FMDV 3C induces the widespread degradation of host proteins through its proteolytic activity and that the apoptosis pathway might be an important strategy to mediate this process. Further exploration of the relationship between apoptosis and degradation induced by 3C could provide novel insights into the pathogenic mechanisms of FMDV. MDPI 2021-11-30 /pmc/articles/PMC8707164/ /pubmed/34959521 http://dx.doi.org/10.3390/pathogens10121566 Text en © 2021 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 Yi, Jiamin Peng, Jiangling Ren, Jingjing Zhu, Guoqiang Ru, Yi Tian, Hong Li, Dan Zheng, Haixue Degradation of Host Proteins and Apoptosis Induced by Foot-and-Mouth Disease Virus 3C Protease |
title | Degradation of Host Proteins and Apoptosis Induced by Foot-and-Mouth Disease Virus 3C Protease |
title_full | Degradation of Host Proteins and Apoptosis Induced by Foot-and-Mouth Disease Virus 3C Protease |
title_fullStr | Degradation of Host Proteins and Apoptosis Induced by Foot-and-Mouth Disease Virus 3C Protease |
title_full_unstemmed | Degradation of Host Proteins and Apoptosis Induced by Foot-and-Mouth Disease Virus 3C Protease |
title_short | Degradation of Host Proteins and Apoptosis Induced by Foot-and-Mouth Disease Virus 3C Protease |
title_sort | degradation of host proteins and apoptosis induced by foot-and-mouth disease virus 3c protease |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8707164/ https://www.ncbi.nlm.nih.gov/pubmed/34959521 http://dx.doi.org/10.3390/pathogens10121566 |
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