Emerging From the Unknown: Structural and Functional Features of Agnoprotein of Polyomaviruses

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• 作者：A. Sami Saribas ; Pascale Coric ; Anahit Hamazaspyan ; William Davis ; Rachael Axman ; Martyn K. White ; Magid Abou-Gharbia ; Wayne Childers ; Jon H. Condra ; Serge Bouaziz and Mahmut Safak
• 刊名：Journal of Cellular Physiology
• 出版年：2016
• 出版时间：October 2016
• 年：2016
• 卷：231
• 期：10
• 页码：2115-2127
• 全文大小：2726K
• ISSN：1097-4652

文摘

Agnoprotein is an important regulatory protein of polyomaviruses, including JCV, BKV, and SV40. In the absence of its expression, these viruses are unable to sustain their productive life cycle. It is a highly basic phosphoprotein that localizes mostly to the perinuclear area of infected cells, although a small amount of the protein is also found in nucleus. Much has been learned about the structure and function of this important regulatory protein in recent years. It forms highly stable dimers/oligomers in vitro and in vivo through its Leu/Ile/Phe-rich domain. Structural NMR studies revealed that this domain adopts an alpha-helix conformation and plays a critical role in the stability of the protein. It associates with cellular proteins, including YB-1, p53, Ku70, FEZ1, HP1α, PP2A, AP-3, PCNA, and α-SNAP; and viral proteins, including small t antigen, large T antigen, HIV-1 Tat, and JCV VP1; and significantly contributes the viral transcription and replication. This review summarizes the recent advances in the structural and functional properties of this important regulatory protein. J. Cell. Physiol. 231: 2115–2127, 2016.