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Chondroitin Sulfate N-acetylgalactosaminyltransferase-2 Contributes to the Replication of Infectious Bursal Disease Virus via Interaction with the Capsid Protein VP2

Infectious bursal disease virus (IBDV) is a birnavirus that causes a highly contagious immunosuppressive disease in young chickens. The capsid protein VP2 of IBDV plays multiple roles in its life cycle. To more comprehensively understand the functions of VP2 involved in the communication between vir...

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Autores principales: Zhang, Lizhou, Ren, Xiangang, Chen, Yuming, Gao, Yulong, Wang, Nian, Lu, Zhen, Gao, Li, Qin, Liting, Wang, Yongqiang, Gao, Honglei, Li, Kai, Jiang, Lili, Cui, Hongyu, Liu, Changjun, Zhang, Yanping, Qi, Xiaole, Wang, Xiaomei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4379581/
https://www.ncbi.nlm.nih.gov/pubmed/25807054
http://dx.doi.org/10.3390/v7031474
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author Zhang, Lizhou
Ren, Xiangang
Chen, Yuming
Gao, Yulong
Wang, Nian
Lu, Zhen
Gao, Li
Qin, Liting
Wang, Yongqiang
Gao, Honglei
Li, Kai
Jiang, Lili
Cui, Hongyu
Liu, Changjun
Zhang, Yanping
Qi, Xiaole
Wang, Xiaomei
author_facet Zhang, Lizhou
Ren, Xiangang
Chen, Yuming
Gao, Yulong
Wang, Nian
Lu, Zhen
Gao, Li
Qin, Liting
Wang, Yongqiang
Gao, Honglei
Li, Kai
Jiang, Lili
Cui, Hongyu
Liu, Changjun
Zhang, Yanping
Qi, Xiaole
Wang, Xiaomei
author_sort Zhang, Lizhou
collection PubMed
description Infectious bursal disease virus (IBDV) is a birnavirus that causes a highly contagious immunosuppressive disease in young chickens. The capsid protein VP2 of IBDV plays multiple roles in its life cycle. To more comprehensively understand the functions of VP2 involved in the communication between virus and host, we used yeast two-hybrid screening to identify the cellular factors that interact with this protein. We found that chondroitin sulfate N-acetylgalactosaminyltransferase-2 (CSGalNAcT2), a typical type II transmembrane protein located in Golgi apparatus, could interact with VP2, and we confirmed this interaction by co-immunoprecipitation and confocal laser scanning microscopy assays. Additionally, up-regulation of CSGalNAcT2 during IBDV infection was observed. Overexpression and siRNA-mediated knockdown of CSGalNAcT2 assays suggested that CSGalNAcT2 promoted IBDV replication. Moreover, this enhancing effect of CSGalNAcT2 could be inhibited by Brefeldin A, which is a Golgi-disturbing agent. This indicated that the integrity of Golgi apparatus structure was involved in the function of CSGalNAcT2. Taken together, we concluded that CSGalNAcT2, located in the Golgi apparatus, contributed to the replication of IBDV via interaction with VP2.
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spelling pubmed-43795812015-05-04 Chondroitin Sulfate N-acetylgalactosaminyltransferase-2 Contributes to the Replication of Infectious Bursal Disease Virus via Interaction with the Capsid Protein VP2 Zhang, Lizhou Ren, Xiangang Chen, Yuming Gao, Yulong Wang, Nian Lu, Zhen Gao, Li Qin, Liting Wang, Yongqiang Gao, Honglei Li, Kai Jiang, Lili Cui, Hongyu Liu, Changjun Zhang, Yanping Qi, Xiaole Wang, Xiaomei Viruses Article Infectious bursal disease virus (IBDV) is a birnavirus that causes a highly contagious immunosuppressive disease in young chickens. The capsid protein VP2 of IBDV plays multiple roles in its life cycle. To more comprehensively understand the functions of VP2 involved in the communication between virus and host, we used yeast two-hybrid screening to identify the cellular factors that interact with this protein. We found that chondroitin sulfate N-acetylgalactosaminyltransferase-2 (CSGalNAcT2), a typical type II transmembrane protein located in Golgi apparatus, could interact with VP2, and we confirmed this interaction by co-immunoprecipitation and confocal laser scanning microscopy assays. Additionally, up-regulation of CSGalNAcT2 during IBDV infection was observed. Overexpression and siRNA-mediated knockdown of CSGalNAcT2 assays suggested that CSGalNAcT2 promoted IBDV replication. Moreover, this enhancing effect of CSGalNAcT2 could be inhibited by Brefeldin A, which is a Golgi-disturbing agent. This indicated that the integrity of Golgi apparatus structure was involved in the function of CSGalNAcT2. Taken together, we concluded that CSGalNAcT2, located in the Golgi apparatus, contributed to the replication of IBDV via interaction with VP2. MDPI 2015-03-23 /pmc/articles/PMC4379581/ /pubmed/25807054 http://dx.doi.org/10.3390/v7031474 Text en © 2015 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 license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Zhang, Lizhou
Ren, Xiangang
Chen, Yuming
Gao, Yulong
Wang, Nian
Lu, Zhen
Gao, Li
Qin, Liting
Wang, Yongqiang
Gao, Honglei
Li, Kai
Jiang, Lili
Cui, Hongyu
Liu, Changjun
Zhang, Yanping
Qi, Xiaole
Wang, Xiaomei
Chondroitin Sulfate N-acetylgalactosaminyltransferase-2 Contributes to the Replication of Infectious Bursal Disease Virus via Interaction with the Capsid Protein VP2
title Chondroitin Sulfate N-acetylgalactosaminyltransferase-2 Contributes to the Replication of Infectious Bursal Disease Virus via Interaction with the Capsid Protein VP2
title_full Chondroitin Sulfate N-acetylgalactosaminyltransferase-2 Contributes to the Replication of Infectious Bursal Disease Virus via Interaction with the Capsid Protein VP2
title_fullStr Chondroitin Sulfate N-acetylgalactosaminyltransferase-2 Contributes to the Replication of Infectious Bursal Disease Virus via Interaction with the Capsid Protein VP2
title_full_unstemmed Chondroitin Sulfate N-acetylgalactosaminyltransferase-2 Contributes to the Replication of Infectious Bursal Disease Virus via Interaction with the Capsid Protein VP2
title_short Chondroitin Sulfate N-acetylgalactosaminyltransferase-2 Contributes to the Replication of Infectious Bursal Disease Virus via Interaction with the Capsid Protein VP2
title_sort chondroitin sulfate n-acetylgalactosaminyltransferase-2 contributes to the replication of infectious bursal disease virus via interaction with the capsid protein vp2
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4379581/
https://www.ncbi.nlm.nih.gov/pubmed/25807054
http://dx.doi.org/10.3390/v7031474
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