Structural Basis of Tetherin Function

Title:Structural Basis of Tetherin Function

Volume: 10 Issue: 4

Author(s): Winfried Weissenhorn, Nolwenn Miguet, Nick Aschman, Patricia Renesto, Yoshiko Usami and Heinrich G. Gottlinger

Affiliation:

Keywords: HIV-1, BST2, tetherin, GPI, Vpu, budding, SAXS, coiled coil, transmembrane, virions

Abstract: HIV-1 employs its structural proteins to orchestrate assembly and budding at the plasma membrane of host cells, which depends on numerous cellular factors. Although cells evolved interferon inducible restriction factors such as tetherin that act as a first line of defense, enveloped viruses, including HIV-1, developed countermeasures in the form of tetherin antagonists such as Vpu that decrease the effect of tetherin and permits normal viral replication in vivo. Here we review recent advances in the understanding of the dynamic structural properties of tetherin that provide the basis to physically retain HIV-1 by bridging plasma and virion membranes after completion of budding.

Cite this article as:

Weissenhorn Winfried, Miguet Nolwenn, Aschman Nick, Renesto Patricia, Usami Yoshiko and G. Gottlinger Heinrich, Structural Basis of Tetherin Function, Current HIV Research 2012; 10 (4) . https://dx.doi.org/10.2174/157016212800792487