Abstract
The interferon-inducible restriction factor tetherin (also known as CD317, BST-2 or HM1.24) has emerged as a key component of the antiviral immune response. Initially, tetherin was shown to restrict replication of various enveloped viruses by inhibiting the release of budding virions from infected cells. More recently, it has become clear that tetherin also acts as a pattern recognition receptor inducing NF-κB-dependent proinflammatory gene expression in virus infected cells. Whereas the ability to restrict virion release is highly conserved among mammalian tetherin orthologs and thus probably an ancient function of this protein, innate sensing seems to be an evolutionarily recent activity. The potent and broad antiviral activity of tetherin is reflected by the fact that many viruses evolved means to counteract this restriction factor. A continuous arms race with viruses has apparently driven the evolution of different isoforms of tetherin with different functional properties. Interestingly, tetherin has also been implicated in cellular processes that are unrelated to immunity, such as the organization of the apical actin network and membrane microdomains or stabilization of the Golgi apparatus. In this review, I summarize our current knowledge of the different functions of tetherin and describe the molecular strategies that viruses have evolved to antagonize or evade this multifunctional host restriction factor.
Highlights
In the late 1960s, researchers estimated that the human genome may contain up to two million protein-coding genes (Kauffman, 1969)
AND CONCLUDING REMARKS The continuous arms race between viruses and their hosts has certainly driven the evolution of the host restriction factor tetherin
Whereas the ability of tetherin to restrict virion release seems to be an ancient function that is highly conserved among all mammalian orthologs, some species have evolved unique features of this protein
Summary
Edited by: Nadine Laguette, Centre National de la Recherche Scientifique, France. Reviewed by: Janet Douglas, Oregon Health & Science University, USA Kei Sato, Institute for Virus Research – Kyoto University, Japan. The interferon-inducible restriction factor tetherin ( known as CD317, BST-2 or HM1.24) has emerged as a key component of the antiviral immune response. Tetherin was shown to restrict replication of various enveloped viruses by inhibiting the release of budding virions from infected cells. It has become clear that tetherin acts as a pattern recognition receptor inducing NF-κB-dependent proinflammatory gene expression in virus infected cells. The potent and broad antiviral activity of tetherin is reflected by the fact that many viruses evolved means to counteract this restriction factor. I summarize our current knowledge of the different functions of tetherin and describe the molecular strategies that viruses have evolved to antagonize or evade this multifunctional host restriction factor
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