BST-2/tetherin: Structural biology, viral antagonism, and immunobiology of a potent host antiviral factor
作者： Tom J. Brett , Melissa Swiecki , Natalie S. Omattage
DOI: 10.1016/J.MOLIMM.2012.11.008
关键词: Function (biology) 、 Viral replication 、 Interferon 、 Structural biology 、 Mechanism (biology) 、 Innate immune system 、 Cell biology 、 Virology 、 Biology 、 Viral envelope 、 Tetherin
摘要: BST-2 (also known as tetherin, CD317, or HM1.24) was first described a potent interferon-inducible host antiviral factor nearly five years ago. Since that time, numerous reports have been published regarding the activity and immunological properties of this protein. blocks viral replication by inhibiting enveloped virus budding from surface infected cells. To counteract this, most viruses developed strategies to antagonize BST-2, each employing unique mechanism. In review, we summarize function, structural biology immunobiology BST-2. Taken together, our current understanding suggests potential avenues well challenges exploiting its action in development broad spectrum treatments.
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