期刊
TRENDS IN MICROBIOLOGY
卷 18, 期 9, 页码 388-396出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.tim.2010.06.010
关键词
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资金
- Public Health Service [AI087498, AI063993, RR000168, AI081668]
- Elizabeth Glaser Pediatric AIDS Foundation
- NATIONAL CENTER FOR RESEARCH RESOURCES [P51RR000168] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R21AI087498, R01AI063993, R01AI095098, R01AI081668, R37AI095098] Funding Source: NIH RePORTER
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.
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