Towards a mechanism of function of the viral ion channel Vpu from HIV-1.

Journal article

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 Vpu(1-81) and a short, the transmembrane (TM) domain comprising peptide Vpu(1-32) 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.

Authors: Mehnert, T; Lam, Y; Judge, P; Routh, A; Fischer, D

• Publication status: Published
• Journal: Journal of biomolecular structure and dynamics
• Volume: 24
• Issue: 6
• Pages: 589-596
• Publication date: 2007-06-01
• DOI: 10.1080/07391102.2007.10507148
• EISSN: 1538-0254
• ISSN: 0739-1102
• Language: English
• Keywords: Human Immunodeficiency Virus Proteins; Electric Conductivity; Ion Channels; Molecular Sequence Data; Peptide Fragments; Kinetics; Recombinant Fusion Proteins; Viral Regulatory and Accessory Proteins; Ion Channel Gating; Amino Acid Sequence; HIV-1