Structural basis of tetherin function

Curr HIV Res. 2012 Jun;10(4):298-306. doi: 10.2174/157016212800792487.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Antigens, CD / genetics*
  • Antigens, CD / ultrastructure
  • Cell Line
  • Female
  • GPI-Linked Proteins / antagonists & inhibitors
  • GPI-Linked Proteins / genetics
  • GPI-Linked Proteins / ultrastructure
  • HIV-1 / immunology*
  • HIV-1 / pathogenicity
  • Host-Pathogen Interactions
  • Human Immunodeficiency Virus Proteins / metabolism
  • Humans
  • Male
  • Mutation*
  • Viral Regulatory and Accessory Proteins / metabolism*
  • Virus Replication

Substances

  • Antigens, CD
  • BST2 protein, human
  • GPI-Linked Proteins
  • Human Immunodeficiency Virus Proteins
  • Viral Regulatory and Accessory Proteins
  • vpu protein, Human immunodeficiency virus 1