Journal
VIROLOGY
Volume 405, Issue 2, Pages 448-456Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2010.06.034
Keywords
Frog virus 3; Iridovirus; Ranavirus; Virion assembly; Antisense morpholino oligonucleotides; Transmission electron microscopy; Immunofluorescence assay; Myristoylated viral protein; Viral membrane protein
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Funding
- NSF [IOS-07-42711]
- School of Graduate Studies, University of Mississippi Medical Center (UMMC)
- Division Of Integrative Organismal Systems
- Direct For Biological Sciences [0742711] Funding Source: National Science Foundation
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Although previous work identified 12 complementation groups with possible roles in virus assembly, currently only one frog virus 3 protein, the major capsid protein (MCP), has been linked with virion formation. To identify other proteins required for assembly, we used an antisense morpholino oligonucleotide to target 53R, a putative myristoylated membrane protein, and showed that treatment resulted in marked reductions in 53R levels and a 60% drop in virus titers. lmmunofluorescence assays confirmed knock down and showed that 53R was found primarily within viral assembly sites, whereas transmission electron microscopy detected fewer mature virions and, in some cells, dense granular bodies that may represent unencapsidated DNA-protein complexes. Treatment with a myristoylation inhibitor (2-hydroxymyristic acid) resulted in an 80% reduction in viral titers. Collectively, these data indicate that 53R is an essential viral protein that is required for replication in vitro and suggest it plays a critical role in virion formation. (C) 2010 Elsevier Inc. All rights reserved.
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