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UL11 Protein Is a Key Participant of the Duck Plague Virus in Its Life Cycle
Tegument protein UL11 plays a critical role in the life cycle of herpesviruses. The UL11 protein of herpesviruses is important for viral particle entry, release, assembly, and secondary envelopment. Lipid raft is cholesterol-rich functional microdomains in cell membranes, which plays an important ro...
Autores principales: | , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8764364/ https://www.ncbi.nlm.nih.gov/pubmed/35058907 http://dx.doi.org/10.3389/fmicb.2021.792361 |
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author | Yang, Linjiang Wang, Mingshu Cheng, Anchun Yang, Qiao Wu, Ying Huang, Juan Tian, Bin Jia, Renyong Liu, Mafeng Zhu, Dekang Chen, Shun Zhao, Xinxin Zhang, Shaqiu Ou, Xumin Mao, Sai Gao, Qun Sun, Di Yu, Yanlin Zhang, Ling |
author_facet | Yang, Linjiang Wang, Mingshu Cheng, Anchun Yang, Qiao Wu, Ying Huang, Juan Tian, Bin Jia, Renyong Liu, Mafeng Zhu, Dekang Chen, Shun Zhao, Xinxin Zhang, Shaqiu Ou, Xumin Mao, Sai Gao, Qun Sun, Di Yu, Yanlin Zhang, Ling |
author_sort | Yang, Linjiang |
collection | PubMed |
description | Tegument protein UL11 plays a critical role in the life cycle of herpesviruses. The UL11 protein of herpesviruses is important for viral particle entry, release, assembly, and secondary envelopment. Lipid raft is cholesterol-rich functional microdomains in cell membranes, which plays an important role in signal transduction and substance transport. Flotillin and prohibition, which are considered to be specific markers of lipid raft. However, little is known about the function of duck plague virus (DPV) UL11 in the life cycle of the viruses and the relationship between the lipid raft and UL11. In this study, an interference plasmid shRNA126 for UL11 was used. Results showed that UL11 is involved in the replication, cell to cell spread, viral particle assembly, and release processes. Furthermore, UL11 was verified that it could interact with the lipid raft through sucrose density gradient centrifugation and that function correlates with the second glycine of the UL11. When the lipid raft was depleted using the methyl-β-cyclodextrin, the release of the DPV was decreased. Moreover, UL11 can decrease several relative viral genes mRNA levels by qRT-PCR and Western blot test. Altogether, these results highlight an important role for UL11 protein in the viral replication cycle. |
format | Online Article Text |
id | pubmed-8764364 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-87643642022-01-19 UL11 Protein Is a Key Participant of the Duck Plague Virus in Its Life Cycle Yang, Linjiang Wang, Mingshu Cheng, Anchun Yang, Qiao Wu, Ying Huang, Juan Tian, Bin Jia, Renyong Liu, Mafeng Zhu, Dekang Chen, Shun Zhao, Xinxin Zhang, Shaqiu Ou, Xumin Mao, Sai Gao, Qun Sun, Di Yu, Yanlin Zhang, Ling Front Microbiol Microbiology Tegument protein UL11 plays a critical role in the life cycle of herpesviruses. The UL11 protein of herpesviruses is important for viral particle entry, release, assembly, and secondary envelopment. Lipid raft is cholesterol-rich functional microdomains in cell membranes, which plays an important role in signal transduction and substance transport. Flotillin and prohibition, which are considered to be specific markers of lipid raft. However, little is known about the function of duck plague virus (DPV) UL11 in the life cycle of the viruses and the relationship between the lipid raft and UL11. In this study, an interference plasmid shRNA126 for UL11 was used. Results showed that UL11 is involved in the replication, cell to cell spread, viral particle assembly, and release processes. Furthermore, UL11 was verified that it could interact with the lipid raft through sucrose density gradient centrifugation and that function correlates with the second glycine of the UL11. When the lipid raft was depleted using the methyl-β-cyclodextrin, the release of the DPV was decreased. Moreover, UL11 can decrease several relative viral genes mRNA levels by qRT-PCR and Western blot test. Altogether, these results highlight an important role for UL11 protein in the viral replication cycle. Frontiers Media S.A. 2022-01-04 /pmc/articles/PMC8764364/ /pubmed/35058907 http://dx.doi.org/10.3389/fmicb.2021.792361 Text en Copyright © 2022 Yang, Wang, Cheng, Yang, Wu, Huang, Tian, Jia, Liu, Zhu, Chen, Zhao, Zhang, Ou, Mao, Gao, Sun, Yu and Zhang. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Yang, Linjiang Wang, Mingshu Cheng, Anchun Yang, Qiao Wu, Ying Huang, Juan Tian, Bin Jia, Renyong Liu, Mafeng Zhu, Dekang Chen, Shun Zhao, Xinxin Zhang, Shaqiu Ou, Xumin Mao, Sai Gao, Qun Sun, Di Yu, Yanlin Zhang, Ling UL11 Protein Is a Key Participant of the Duck Plague Virus in Its Life Cycle |
title | UL11 Protein Is a Key Participant of the Duck Plague Virus in Its Life Cycle |
title_full | UL11 Protein Is a Key Participant of the Duck Plague Virus in Its Life Cycle |
title_fullStr | UL11 Protein Is a Key Participant of the Duck Plague Virus in Its Life Cycle |
title_full_unstemmed | UL11 Protein Is a Key Participant of the Duck Plague Virus in Its Life Cycle |
title_short | UL11 Protein Is a Key Participant of the Duck Plague Virus in Its Life Cycle |
title_sort | ul11 protein is a key participant of the duck plague virus in its life cycle |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8764364/ https://www.ncbi.nlm.nih.gov/pubmed/35058907 http://dx.doi.org/10.3389/fmicb.2021.792361 |
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