Assembling viral channel forming proteins: Vpu from HIV-1

Li Hua Li, Hao Jen Hsu, Wolfgang B. Fischer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


Different routes of assembly are probed for the transmembrane domain (TMD) of the bitopic membrane protein Vpu from HIV-1. Vpu is responsible for the amplification of viral release from the host cell. The mode of action includes (i) heteroassembly with host factors and (ii) the formation of homo-oligomers, which are able to conduct ions across the lipid membrane. Two different routes of assembling short sequences of the N terminus, including the TMD of Vpu, Vpu1-32, and Vpu8-26, are presented by using a combination of classical molecular dynamics (MD) simulations combined with a docking approach. The rim of alanines (Ala-8, -11, -15, and -19) resembles an interlocking motif for the sequential assembly into a dimer and trimer. Simultaneous assembly results in oligomeric bundles (trimers to pentamers) with either tryptophans (Trp-23) or purely hydrophobic residues facing the center. Bundles, with serines facing the pore (Ser-24), are energetically not the lowest structures. For pentameric bundles with Ser-24 facing the pore, no water column develops during a short 25 ns MD simulation.

Original languageEnglish
Pages (from-to)517-529
Number of pages13
Issue number8
StatePublished - Aug 2013


  • assembly
  • docking approach
  • membrane protein
  • molecular dynamics simulations
  • Vpu HIV-1


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