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

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

doi:10.1002/prot.21642

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

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

Research output: Contribution to journal › Article › peer-review

57 Scopus citations

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 (Vpu_1-32-W23L, Vpu _1-32-R31V, Vpu_1-32-S24L) have been synthesized and reconstituted into artificial lipid bilayers. All peptides show channel activity with a main conductance level of around 20 pS. Vpu_1-32-W23L has a considerable flickering pattern in the recordings and longer open times than Vpu_1-32. Whilst recordings for Vpu_1-32-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 Vpu_1-32-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 language	English (US)
Pages (from-to)	1488-1497
Number of pages	10
Journal	Proteins: Structure, Function and Genetics
Volume	70
Issue number	4
DOIs	https://doi.org/10.1002/prot.21642
State	Published - Mar 2008
Externally published	Yes

Keywords

Artificial bilayers
Gating
HIV-1
Ion channels
Membrane proteins
Vpu

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

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10.1002/prot.21642

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title = "Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism",

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.",

keywords = "Artificial bilayers, Gating, HIV-1, Ion channels, Membrane proteins, Vpu",

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AU - Mehnert, T.

AU - Routh, A.

AU - Judge, P. J.

AU - Lam, Y. H.

AU - Fischer, D.

AU - Watts, A.

AU - Fischer, W. B.

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N2 - 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.

AB - 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.

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KW - Membrane proteins

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

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Keywords

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