BST-2/tetherin: a new component of the innate immune response to enveloped viruses

被引:164
作者
Evans, David T. [1 ]
Serra-Moreno, Ruth [1 ]
Singh, Rajendra K. [2 ]
Guatelli, John C. [2 ,3 ]
机构
[1] Harvard Univ, Sch Med, New England Primate Res Ctr, Dept Microbiol & Mol Genet, Southborough, MA 01772 USA
[2] Univ Calif San Diego, Dept Med, La Jolla, CA 92093 USA
[3] VA San Diego Healthcare Syst, San Diego, CA 92161 USA
关键词
SIMIAN-IMMUNODEFICIENCY-VIRUS; CELL-SURFACE; MOLECULAR-CLONING; PARTICLE RELEASE; HIV-1; INFECTION; DOWN-MODULATION; BETA-TRCP; VPU GENE; RESTRICTION; PROTEIN;
D O I
10.1016/j.tim.2010.06.010
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The 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.
引用
收藏
页码:388 / 396
页数:9
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