{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,7]],"date-time":"2026-02-07T16:48:46Z","timestamp":1770482926824,"version":"3.49.0"},"reference-count":45,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[2011,3,15]],"date-time":"2011-03-15T00:00:00Z","timestamp":1300147200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2011,3,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>BST-2\/CD317\/tetherin is a host factor that inhibits the release of HIV-1 and other unrelated viruses. A current model proposes that BST-2 physically tethers virions to the surface of virus-producing cells. The HIV-1-encoded Vpu protein effectively antagonizes the activity of BST-2. How Vpu accomplishes this task remains unclear; however, it is known that Vpu has the ability to down-modulate BST-2 from the cell surface. Here we analyzed the effects of Vpu on BST-2 by performing a series of kinetic studies with HeLa, 293T, and CEMx174 cells. Our results indicate that the surface downregulation of BST-2 is not due to an accelerated internalization or reduced recycling of internalized BST-2 but instead is caused by interference with the resupply of newly synthesized BST-2 from within the cell. While our data confirm previous reports that the high-level expression of Vpu can cause the endoplasmic reticulum (ER)-associated degradation of BST-2, we found no evidence that Vpu targets endogenous BST-2 in the ER in the course of a viral infection. Instead, we found that Vpu acts in a post-ER compartment and increases the turnover of newly synthesized mature BST-2. Our observation that Vpu does not affect the recycling of BST-2 suggests that Vpu does not act directly at the cell surface but may interfere with the trafficking of newly synthesized BST-2 to the cell surface, resulting in the accelerated targeting of BST-2 to the lysosomal compartment for degradation.<\/jats:p>","DOI":"10.1128\/jvi.02080-10","type":"journal-article","created":{"date-parts":[[2010,12,30]],"date-time":"2010-12-30T01:48:28Z","timestamp":1293673708000},"page":"2611-2619","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":43,"title":["Differential Effects of Human Immunodeficiency Virus Type 1 Vpu on the Stability of BST-2\/Tetherin"],"prefix":"10.1128","volume":"85","author":[{"given":"Amy J.","family":"Andrew","sequence":"first","affiliation":[{"name":"Laboratory of Molecular Microbiology, Viral Biochemistry Section, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, Maryland 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