Journal
VIROLOGY
Volume 443, Issue 1, Pages 161-176Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2013.05.003
Keywords
Polyomavirus JCV; SV40; BKV; Merkel cell carcinoma virus; Large T antigen; Agnoprotein; Transcription; DNA replication; Progressive multifocal leukoencephalopathy; Splicing; Stable dimer formation; Stable oligomer formation
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Funding
- NIH
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Agnoprotein is one of the key regulatory proteins of polyomaviruses, including JCV, BKV and SV40 and is required for a productive viral life cycle. We have recently reported that agnoprotein forms stable dimer/oligomers mediated by a predicted amphipathic alpha-helix, spanning amino acids (aa), 17 to 42. Deletion of the alpha-helix renders a replication incompetent virus. Here, we have further characterized this region by a systematic deletion and substitution mutagenesis and demonstrated that a Leu/Ile/Phe-rich domain, (spanning aa 28-39) within alpha-helix is indispensable for agnoprotein structure and function. Deletion of aa 30-37 severely affects the dimer/oligomer formation and stable expression of the protein. Mutagenesis data also indicate that the residues, 34-36, may be involved in regulation of the splicing events of JCV transcripts. Collectively, these data suggest that the Leu/Ile/Phe-rich domain plays critical roles in agnoprotein function and thus represents a potential target for developing novel therapeutics against JCV infections. (C) 2013 Elsevier Inc. All rights reserved.
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