The interferon-inducible protein tetherin (also called BST2, CD317, or HM1.24) is a key component of the innate immunity against retroviral infections. Tetherin was named after its unique ability to restrict the release of enveloped viruses by physically tethering them to the plasma membrane of infected cells. Notably, tetherin also acts as a pattern recognition receptor inducing NF-κB-dependent expression of antiviral genes upon sensing of budding virions.
At least three primate lentiviral proteins (Vpu, Nef, and Env) have evolved the ability to counteract tetherin and enable the virus to evade this restriction. Due to a constant evolutionary arms race between virus and host, antagonization of tetherin by viral proteins is frequently species-specific. Human tetherin, for example, is resistant against counteraction by many simian immunodeficiency viruses (SIV) and represents a significant hurdle for successful zoonotic transmissions of SIV to humans. Thus, the evolution of a...
KeywordsCodon Tyrosine Leukemia Cysteine Interferon
- Sauter D, Hotter D, Van Driessche B et al. Differential regulation of NF-κB-mediated proviral and antiviral host gene expression by primate lentiviral Nef and Vpu proteins. Cell Rep. 2015;10(4):586–99.Google Scholar
- Tavano B, Galao RP, Graham DR, et al. Ig-like transcript 7, but not bone marrow stromal cell antigen 2 (also known as HM1.24, tetherin, or CD317), modulates plasmacytoid dendritic cell function in primary human blood leukocytes. J Immunol Baltim Md 1950. 2013;190:2622–30. doi:10.4049/jimmunol.1202391.Google Scholar