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Virologie. Volume 16, Number 1, 32-42, Janvier-Février 2012, revue

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Author(s) : Nicolas Aschman, Winfried Weissenhorn, Patricia Renesto

Summary : Tetherin is an unusual surface glycoprotein that employs an N-terminal and a C-terminal region to anchor the protein into membranes. Structural analyses revealed an elongated structure for the ectodomain that is probably oriented parallel to cellular membranes. Expression of tetherin can be induced by interferon in selected cell types, which leads to the restriction of HIV-1 replication in the absence of the viral antagonist Vpu. This review focuses on recent progress on the understanding of the molecular mechanisms of tetherin function during HIV and other enveloped virus budding processes. We discuss the role of diverse viral antagonists in tetherin down regulation and place the structural information on the ectodomain into the context of tetherin's ability to physically link virions such as HIV-1 to the plasma membrane after completion of budding.

Keywords : HIV-1, tetherin, BST-2, Vpu, Nef