ArticleVirology journal2012
Characterization of grass carp reovirus minor core protein VP4.
Article in Virology journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 30 citations in OpenAlex.
- Grass carp reovirus VP4 manipulates TOLLIP to degrade STING for inhibition of IFN production.Journal of virology · 2025Article
- Article
- Hypoxia triggers the outbreak of infectious spleen and kidney necrosis virus disease through viral hypoxia response elements.Virulence · 2022Article
- Oral Administration ofViruses · 2021Article
- Oral Vaccination of Grass Carp (Vaccines · 2021Article
- A Novel Subunit Vaccine Based on Outer Capsid Proteins of Grass Carp Reovirus (GCRV) Provides Protective Immunity against GCRV Infection in Rare Minnow (Pathogens (Basel, Switzerland) · 2020Article
- The N-Terminal of Aquareovirus NS80 Is Required for Interacting with Viral Proteins and Viral Replication.PloS one · 2016Article
- Article
- Pathogenicity and tissue distribution of grass carp reovirus after intraperitoneal administration.Virology journal · 2014Article
- The VP2 protein of grass carp reovirus (GCRV) expressed in a baculovirus exhibits RNA polymerase activity.Virologica Sinica · 2014Article
- Aquareovirus protein VP6 colocalizes with NS80 protein in infected and transfected cells.Virology journal · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundGrass Carp Reovirus (GCRV), a tentative member in the genus Aquareovirus of family Reoviridae, contains eleven segmented (double-stranded RNA) dsRNA genome which encodes 12 proteins. A low-copy core component protein VP4, encoded by the viral genome segment 5(S5), has been suggested to play a key role in viral genome transcription and replication.
resultsTo understand the role of minor core protein VP4 played in molecular pathogenesis during GCRV infection, the recombinant GCRV VP4 gene was constructed and expressed in both prokaryotic and mammalian cells in this investigation. The recombinant His-tag fusion VP4 products expressed in E.coli were identified by Western blotting utilizing His-tag specific monoclonal and GCRV polyclonal antibodies. In addition, the expression of VP4 in GCRV infected cells, appeared in granules structure concentrated mainly in the cytoplasm, can be detected by Immunofluorescence (IF) using prepared anti-VP4 polyclonal antibody. Meanwhile, VP4 protein in GCRV core and infected cell lysate was identified by Immunoblotting (IB) assay. Of particular note, the VP4 protein was exhibited a diffuse distribution in the cytoplasm and nucleus in transfected cells, suggesting that VP4 protein may play a partial role in the nucleus by regulating cell cycle besides its predicted cytoplasmic function in GCRV infection.
conclusionsOur results indicate the VP4 is a core component in GCRV. The cellular localization of VP4 is correlated with its predicted function. The data provide a foundation for further studies aimed at understanding the role of VP4 in viroplasmic inclusion bodies (VIB) formation during GCRV replication and assembly.
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