Please use this identifier to cite or link to this item: https://doi.org/10.1038/srep13151
Title: Singapore Grouper Iridovirus ORF75R is a Scaffold Protein Essential for Viral Assembly
Authors: Wang F. 
Liu Y.
Zhu Y.
Ngoc Tran B. 
Wu J. 
Leong Hew C. 
Keywords: adenosine triphosphate
lipid bilayer
magnesium
viral protein
drug effects
gene silencing
Iridovirus
lipid bilayer
metabolism
pathogenicity
phosphorylation
physiology
virion
virus assembly
virus capsid
virus infection
Adenosine Triphosphate
Capsid
Gene Knockdown Techniques
Iridovirus
Lipid Bilayers
Magnesium
Phosphorylation
Viral Proteins
Virion
Virus Assembly
Virus Diseases
Issue Date: 2015
Publisher: Nature Publishing Group
Citation: Wang F., Liu Y., Zhu Y., Ngoc Tran B., Wu J., Leong Hew C. (2015). Singapore Grouper Iridovirus ORF75R is a Scaffold Protein Essential for Viral Assembly. Scientific Reports 5 : 13151. ScholarBank@NUS Repository. https://doi.org/10.1038/srep13151
Abstract: Singapore Grouper Iridovirus (SGIV) is a member of nucleo cytoplasmic large DNA viruses (NCLDV). This paper reports the functional analysis of ORF75R, a major structural protein of SGIV. Immuno fluorescence studies showed that the protein was accumulated in the viral assembly site. Immunogold-labelling indicated that it was localized between the viral capsid shell and DNA core. Knockdown of ORF75R by morpholinos resulted in the reduction of coreshell thickness, the failure of DNA encapsidation, and the low yield of infectious particles. Comparative proteomics further identified the structural proteins affected by ORF75R knockdown. Two-dimensional gel electrophoresis combined with proteomics demonstrated that ORF75R was phosphorylated at multiple sites in SGIV-infected cell lysate and virions, but the vast majority of ORF75R in virions was the dephosphorylated isoform. A kinase assay showed that ORF75R could be phosphorylated in vitro by the SGIV structural protein ORF39L. Addition of ATP and Mg2+ into purified virions prompted extensive phosphorylation of structural proteins and release of ORF75R from virions. These data suggest that ORF75R is a novel scaffold protein important for viral assembly and DNA encapsidation, but its phosphorylation facilitates virion disassembly. Compared to proteins from other viruses, we found that ORF75R shares common features with herpes simplex virus VP22.
Source Title: Scientific Reports
URI: https://scholarbank.nus.edu.sg/handle/10635/175490
ISSN: 20452322
DOI: 10.1038/srep13151
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