Structural Basis of Tetherin Function
Winfried Weissenhorn, Nolwenn Miguet, Nick Aschman, Patricia Renesto, Yoshiko Usami and Heinrich G. Gottlinger
Affiliation: Unit of Virus Host Cell Interactions (UVHCI) UMI 3265 Universite Joseph Fourier-EMBL-CNRS, 6 rue Jules Horowitz, 38042 Grenoble Cedex 9, France.
Keywords: HIV-1, BST2, tetherin, GPI, Vpu, budding, SAXS, coiled coil, transmembrane, virions
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.
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