The N-Terminal of Aquareovirus NS80 Is Required for Interacting with Viral Proteins and Viral Replication
Reovirus replication and assembly occurs within viral inclusion bodies that formed in specific intracellular compartments of cytoplasm in infected cells. Previous study indicated that aquareovirus NS80 is able to form inclusion bodies, and also can retain viral proteins within its inclusions. To bet...
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pubmed-47522862016-02-26 The N-Terminal of Aquareovirus NS80 Is Required for Interacting with Viral Proteins and Viral Replication Zhang, Jie Guo, Hong Chen, Qingxiu Zhang, Fuxian Fang, Qin Research Article Reovirus replication and assembly occurs within viral inclusion bodies that formed in specific intracellular compartments of cytoplasm in infected cells. Previous study indicated that aquareovirus NS80 is able to form inclusion bodies, and also can retain viral proteins within its inclusions. To better understand how NS80 performed in viral replication and assembly, the functional regions of NS80 associated with other viral proteins in aquareovirus replication were investigated in this study. Deletion mutational analysis and rotavirus NSP5-based protein association platform were used to detect association regions. Immunofluorescence images indicated that different N-terminal regions of NS80 could associate with viral proteins VP1, VP4, VP6 and NS38. Further co-immunoprecipitation analysis confirmed the interaction between VP1, VP4, VP6 or NS38 with different regions covering the N-terminal amino acid (aa, 1–471) of NS80, respectively. Moreover, removal of NS80 N-terminal sequences required for interaction with proteins VP1, VP4, VP6 or NS38 not only prevented the capacity of NS80 to support viral replication in NS80 shRNA-based replication complementation assays, but also inhibited the expression of aquareovirus proteins, suggesting that N-terminal regions of NS80 are necessary for viral replication. These results provided a foundational basis for further understanding the role of NS80 in viral replication and assembly during aquareovirus infection. Public Library of Science 2016-02-12 /pmc/articles/PMC4752286/ /pubmed/26871941 http://dx.doi.org/10.1371/journal.pone.0148550 Text en © 2016 Zhang et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
repository_type |
Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Zhang, Jie Guo, Hong Chen, Qingxiu Zhang, Fuxian Fang, Qin |
spellingShingle |
Zhang, Jie Guo, Hong Chen, Qingxiu Zhang, Fuxian Fang, Qin The N-Terminal of Aquareovirus NS80 Is Required for Interacting with Viral Proteins and Viral Replication |
author_facet |
Zhang, Jie Guo, Hong Chen, Qingxiu Zhang, Fuxian Fang, Qin |
author_sort |
Zhang, Jie |
title |
The N-Terminal of Aquareovirus NS80 Is Required for Interacting with Viral Proteins and Viral Replication |
title_short |
The N-Terminal of Aquareovirus NS80 Is Required for Interacting with Viral Proteins and Viral Replication |
title_full |
The N-Terminal of Aquareovirus NS80 Is Required for Interacting with Viral Proteins and Viral Replication |
title_fullStr |
The N-Terminal of Aquareovirus NS80 Is Required for Interacting with Viral Proteins and Viral Replication |
title_full_unstemmed |
The N-Terminal of Aquareovirus NS80 Is Required for Interacting with Viral Proteins and Viral Replication |
title_sort |
n-terminal of aquareovirus ns80 is required for interacting with viral proteins and viral replication |
description |
Reovirus replication and assembly occurs within viral inclusion bodies that formed in specific intracellular compartments of cytoplasm in infected cells. Previous study indicated that aquareovirus NS80 is able to form inclusion bodies, and also can retain viral proteins within its inclusions. To better understand how NS80 performed in viral replication and assembly, the functional regions of NS80 associated with other viral proteins in aquareovirus replication were investigated in this study. Deletion mutational analysis and rotavirus NSP5-based protein association platform were used to detect association regions. Immunofluorescence images indicated that different N-terminal regions of NS80 could associate with viral proteins VP1, VP4, VP6 and NS38. Further co-immunoprecipitation analysis confirmed the interaction between VP1, VP4, VP6 or NS38 with different regions covering the N-terminal amino acid (aa, 1–471) of NS80, respectively. Moreover, removal of NS80 N-terminal sequences required for interaction with proteins VP1, VP4, VP6 or NS38 not only prevented the capacity of NS80 to support viral replication in NS80 shRNA-based replication complementation assays, but also inhibited the expression of aquareovirus proteins, suggesting that N-terminal regions of NS80 are necessary for viral replication. These results provided a foundational basis for further understanding the role of NS80 in viral replication and assembly during aquareovirus infection. |
publisher |
Public Library of Science |
publishDate |
2016 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4752286/ |
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1613538069834629120 |