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lüll BST-2/tetherin: a new component of the innate immune response to enveloped viruses Evans DT; Serra-Moreno R; Singh RK; Guatelli JCTrends Microbiol 2010[Sep]; 18 (9): 388-96The interferon-inducible, transmembrane protein BST-2 (CD317, tetherin) directly holds fully formed enveloped virus particles to the cells that produce them, inhibiting their spread. BST-2 inhibits members of the retrovirus, filovirus, arenavirus and herpesvirus families. These viruses encode a variety of proteins to degrade BST-2 and/or direct it away from its site of action at the cell surface. Viral antagonism has subjected BST-2 to positive selection, leading to species-specific differences that presented a barrier to the transmission of simian immunodeficiency viruses (SIVs) to humans. This barrier was crossed by HIV-1 when its Vpu protein acquired activity as a BST-2 antagonist. Here, we review this new host-pathogen relationship and discuss its impact on the evolution of primate lentiviruses and the origins of the HIV pandemic.|*Immunity, Innate[MESH]|Acquired Immunodeficiency Syndrome/epidemiology/virology[MESH]|Animals[MESH]|Antigens, CD/chemistry/immunology/*metabolism[MESH]|Cell Membrane/immunology/virology[MESH]|Evolution, Molecular[MESH]|GPI-Linked Proteins[MESH]|HIV-1/*immunology/metabolism/*physiology[MESH]|Host-Pathogen Interactions[MESH]|Human Immunodeficiency Virus Proteins/*metabolism[MESH]|Humans[MESH]|Lentiviruses, Primate/genetics/immunology/*physiology[MESH]|Membrane Glycoproteins/antagonists & inhibitors/chemistry/*metabolism[MESH]|Primates[MESH]|Simian Immunodeficiency Virus/physiology[MESH]|Viral Envelope Proteins/immunology/metabolism[MESH]|Viral Regulatory and Accessory Proteins/*metabolism[MESH] |