Nature Communications (Nov 2017)

Tsg101 chaperone function revealed by HIV-1 assembly inhibitors

  • Madeleine Strickland,
  • Lorna S. Ehrlich,
  • Susan Watanabe,
  • Mahfuz Khan,
  • Marie-Paule Strub,
  • Chi-Hao Luan,
  • Michael D. Powell,
  • Jonathan Leis,
  • Nico Tjandra,
  • Carol A. Carter

DOI
https://doi.org/10.1038/s41467-017-01426-2
Journal volume & issue
Vol. 8, no. 1
pp. 1 – 12

Abstract

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Tsg101 is a component of the host cellular ESCRT machinery and is required for HIV-1 replication. Here, the authors show that disruption of ubiquitin binding of the Tsg101 UEV domain through commonly used drugs arrests virus assembly, which might facilitate the development of potent HIV inhibitors.