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African Swine Fever Virus Structural Protein p17 Inhibits cGAS-STING Signaling Pathway Through Interacting With STING
African swine fever virus (ASFV) encodes more than 150 proteins, which establish complex interactions with the host for the benefit of the virus in order to evade the host’s defenses. However, currently, there is still a lack of information regarding the roles of the viral proteins in host cells. He...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9283692/ https://www.ncbi.nlm.nih.gov/pubmed/35844609 http://dx.doi.org/10.3389/fimmu.2022.941579 |
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author | Zheng, Wanglong Xia, Nengwen Zhang, Jiajia Cao, Qi Jiang, Sen Luo, Jia Wang, Hui Chen, Nanhua Zhang, Quan Meurens, François Zhu, Jianzhong |
author_facet | Zheng, Wanglong Xia, Nengwen Zhang, Jiajia Cao, Qi Jiang, Sen Luo, Jia Wang, Hui Chen, Nanhua Zhang, Quan Meurens, François Zhu, Jianzhong |
author_sort | Zheng, Wanglong |
collection | PubMed |
description | African swine fever virus (ASFV) encodes more than 150 proteins, which establish complex interactions with the host for the benefit of the virus in order to evade the host’s defenses. However, currently, there is still a lack of information regarding the roles of the viral proteins in host cells. Here, our data demonstrated that ASFV structural protein p17 exerts a negative regulatory effect on cGAS-STING signaling pathway and the STING signaling dependent anti-HSV1 and anti-VSV functions. Further, the results indicated that ASFV p17 was located in ER and Golgi apparatus, and interacted with STING. ASFV p17 could interfere the STING to recruit TBK1 and IKKϵ through its interaction with STING. It was also suggested that the transmembrane domain (amino acids 39–59) of p17 is required for interacting with STING and inhibiting cGAS-STING pathway. Additionally, with the p17 specific siRNA, the ASFV induced IFN-β, ISG15, ISG56, IL-6 and IL-8 gene transcriptions were upregulated in ASFV infected primary porcine alveolar macrophages (PAMs). Taken together, ASFV p17 can inhibit the cGAS-STING pathway through its interaction with STING and interference of the recruitment of TBK1 and IKKϵ. Our work establishes the role of p17 in the immune evasion and thus provides insights on ASFV pathogenesis. |
format | Online Article Text |
id | pubmed-9283692 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-92836922022-07-16 African Swine Fever Virus Structural Protein p17 Inhibits cGAS-STING Signaling Pathway Through Interacting With STING Zheng, Wanglong Xia, Nengwen Zhang, Jiajia Cao, Qi Jiang, Sen Luo, Jia Wang, Hui Chen, Nanhua Zhang, Quan Meurens, François Zhu, Jianzhong Front Immunol Immunology African swine fever virus (ASFV) encodes more than 150 proteins, which establish complex interactions with the host for the benefit of the virus in order to evade the host’s defenses. However, currently, there is still a lack of information regarding the roles of the viral proteins in host cells. Here, our data demonstrated that ASFV structural protein p17 exerts a negative regulatory effect on cGAS-STING signaling pathway and the STING signaling dependent anti-HSV1 and anti-VSV functions. Further, the results indicated that ASFV p17 was located in ER and Golgi apparatus, and interacted with STING. ASFV p17 could interfere the STING to recruit TBK1 and IKKϵ through its interaction with STING. It was also suggested that the transmembrane domain (amino acids 39–59) of p17 is required for interacting with STING and inhibiting cGAS-STING pathway. Additionally, with the p17 specific siRNA, the ASFV induced IFN-β, ISG15, ISG56, IL-6 and IL-8 gene transcriptions were upregulated in ASFV infected primary porcine alveolar macrophages (PAMs). Taken together, ASFV p17 can inhibit the cGAS-STING pathway through its interaction with STING and interference of the recruitment of TBK1 and IKKϵ. Our work establishes the role of p17 in the immune evasion and thus provides insights on ASFV pathogenesis. Frontiers Media S.A. 2022-07-01 /pmc/articles/PMC9283692/ /pubmed/35844609 http://dx.doi.org/10.3389/fimmu.2022.941579 Text en Copyright © 2022 Zheng, Xia, Zhang, Cao, Jiang, Luo, Wang, Chen, Zhang, Meurens and Zhu 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 | Immunology Zheng, Wanglong Xia, Nengwen Zhang, Jiajia Cao, Qi Jiang, Sen Luo, Jia Wang, Hui Chen, Nanhua Zhang, Quan Meurens, François Zhu, Jianzhong African Swine Fever Virus Structural Protein p17 Inhibits cGAS-STING Signaling Pathway Through Interacting With STING |
title | African Swine Fever Virus Structural Protein p17 Inhibits cGAS-STING Signaling Pathway Through Interacting With STING |
title_full | African Swine Fever Virus Structural Protein p17 Inhibits cGAS-STING Signaling Pathway Through Interacting With STING |
title_fullStr | African Swine Fever Virus Structural Protein p17 Inhibits cGAS-STING Signaling Pathway Through Interacting With STING |
title_full_unstemmed | African Swine Fever Virus Structural Protein p17 Inhibits cGAS-STING Signaling Pathway Through Interacting With STING |
title_short | African Swine Fever Virus Structural Protein p17 Inhibits cGAS-STING Signaling Pathway Through Interacting With STING |
title_sort | african swine fever virus structural protein p17 inhibits cgas-sting signaling pathway through interacting with sting |
topic | Immunology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9283692/ https://www.ncbi.nlm.nih.gov/pubmed/35844609 http://dx.doi.org/10.3389/fimmu.2022.941579 |
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