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...

Full description

Bibliographic Details
Main Authors: Zhang, Jie, Guo, Hong, Chen, Qingxiu, Zhang, Fuxian, Fang, Qin
Format: Online
Language:English
Published: Public Library of Science 2016
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4752286/
id pubmed-4752286
recordtype oai_dc
spelling 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/
_version_ 1613538069834629120