Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism

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

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

Vpu from HIV-1 is an 81 amino acid type I integral membrane protein which consists of a cytoplasmic and a transmembrane (TM) domain. The TM domain is known to alter membrane permeability for ions and substrates when inserted into artificial membranes. Peptides corresponding to the TM domain of Vpu (Vpu 1-32) and mutant peptides (Vpu1-32-W23L, Vpu 1-32-R31V, Vpu1-32-S24L) have been synthesized and reconstituted into artificial lipid bilayers. All peptides show channel activity with a main conductance level of around 20 pS. Vpu1-32-W23L has a considerable flickering pattern in the recordings and longer open times than Vpu1-32. Whilst recordings for Vpu1-32-R31V are almost indistinguishable from those of the WT peptide, recordings for Vpu 1-32-S24L do not exhibit any noticeable channel activity. Recordings of WT peptide and Vpu1-32-W23L indicate Michaelis-Menten behavior when the salt concentration is increased. Both peptide channels follow the Eisenman series I, indicative for a weak ion channel with almost pore like characteristics.

Original languageEnglish (US)
Pages (from-to)1488-1497
Number of pages10
JournalProteins: Structure, Function and Genetics
Volume70
Issue number4
DOIs
StatePublished - Mar 2008
Externally publishedYes

Fingerprint

HIV-1
Peptides
Flickering
Artificial Membranes
Membranes
Lipid bilayers
Lipid Bilayers
Ion Channels
Permeability
Membrane Proteins
Salts
Ions
Amino Acids
Substrates
peptide 32

Keywords

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

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

Mehnert, T., Routh, A., Judge, P. J., Lam, Y. H., Fischer, D., Watts, A., & Fischer, W. B. (2008). Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism. Proteins: Structure, Function and Genetics, 70(4), 1488-1497. https://doi.org/10.1002/prot.21642

Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism. / Mehnert, T.; Routh, Andrew; Judge, P. J.; Lam, Y. H.; Fischer, D.; Watts, A.; Fischer, W. B.

In: Proteins: Structure, Function and Genetics, Vol. 70, No. 4, 03.2008, p. 1488-1497.

Research output: Contribution to journalArticle

Mehnert, T, Routh, A, Judge, PJ, Lam, YH, Fischer, D, Watts, A & Fischer, WB 2008, 'Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism', Proteins: Structure, Function and Genetics, vol. 70, no. 4, pp. 1488-1497. https://doi.org/10.1002/prot.21642
Mehnert, T. ; Routh, Andrew ; Judge, P. J. ; Lam, Y. H. ; Fischer, D. ; Watts, A. ; Fischer, W. B. / Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism. In: Proteins: Structure, Function and Genetics. 2008 ; Vol. 70, No. 4. pp. 1488-1497.
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