Viperin is a recently identified putative radical S-adenosylmethionine (SAM)-dependent enzyme that is involved in the cellular antiviral response.  It is one of the interferon-stimulated genes (ISGs), activated as a part of the innate immune system. However, the biochemical role of viperin in the innate immunity signaling pathway is still unclear. Because Toll-like receptor 7 (TLR7) and Toll-like receptor 9 (TLR9) sense viral nucleic acids and promote type I interferon production during viral infection, viperin is predicted to be a key component in these signaling pathways. It recruits the signaling proteins to lipid bodies, and thereby facilitates the downstream activation process. Here, we studied the interaction of viperin with tumor necrosis factor (TNF) receptor associated factor 6 (TRAF6), one of the key proteins in the signaling complex. TRAF6 mediates the signal through the ubiquitination of interleukin 1 receptor associated kinase 1 (IRAK1). We present studies on the interaction of viperin with TRAF6, and examine how this interaction affects the ubiquitination activity of TRAF6 and the radical SAM activity of viperin.

Understanding the role of TRAF6 in the antiviral activity of Viperin

254th National Meeting (2017)

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