Towards a mechanism of function of the viral ion channel vpu from hiv-1

T. Mehnert, Y. H. Lam, P. J. Judge, A. Routh, D. Fischer, A. Watts, W. B. Fischer

Research output: Contribution to journalArticlepeer-review

24 Scopus citations


Vpu, an integral membrane protein encoded in HIV-1, is implicated in the release of new virus particles from infected cells, presumably mediated by ion channel activity of homo-oligomeric Vpu bundles. Reconstitution of both full length Vpu1–81 and a short, the transmembrane (TM) domain comprising peptide Vpu1-32 into bilayers under a constant electric field results in an asymmetric orientation of those channels. For both cases, channel activity with similar kinetics is observed. Channels can open and remain open within a broad series of conductance states even if a small or no electric potential is applied. The mean open time for Vpu peptide channels is voltage-independent. The rate of channel opening shows a biphasic voltage activation, implicating that the gating is influenced by the interaction of the dipole moments of the TM helices with an electric field.

Original languageEnglish (US)
Pages (from-to)589-596
Number of pages8
JournalJournal of Biomolecular Structure and Dynamics
Issue number6
StatePublished - Jun 2007
Externally publishedYes


  • Gating
  • HIV-1
  • Ion channels
  • Membrane proteins
  • Vpu

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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