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Current HIV Research
ISSN (Print): 1570-162X
ISSN (Online): 1873-4251
VOLUME: 10
ISSUE: 4
DOI: 10.2174/157016212800792487      Price:  $58









Structural Basis of Tetherin Function

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Author(s): Winfried Weissenhorn, Nolwenn Miguet, Nick Aschman, Patricia Renesto, Yoshiko Usami and Heinrich G. Gottlinger
Pages 298-306 (9)
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.
Keywords:
HIV-1, BST2, tetherin, GPI, Vpu, budding, SAXS, coiled coil, transmembrane, virions
Affiliation:
Unit of Virus Host Cell Interactions (UVHCI) UMI 3265 Universite Joseph Fourier-EMBL-CNRS, 6 rue Jules Horowitz, 38042 Grenoble Cedex 9, France.