Modulating the activity of the channel-forming segment of Vpr protein from HIV-1

Chin Pei Chen; Clemens Kremer; Peter Henklein; Ulrich Schubert; Rainer H.A. Fink; Wolfgang B. Fischer

doi:10.1007/s00249-009-0518-x

Modulating the activity of the channel-forming segment of Vpr protein from HIV-1

Chin Pei Chen, Clemens Kremer, Peter Henklein, Ulrich Schubert, Rainer H.A. Fink, Wolfgang B. Fischer

Institute of Biophotonics

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

4 Scopus citations

Abstract

Viral protein of regulation (V_pr) encoded by human immunodeficiency virus type 1 (HIV-1) is a short auxiliary protein that is 96 amino acids in length. During the viral life cycle, Vpr is released into the blood serum and is able to enter cellular membranes of noninfected cells. In this study a short peptide, V_pr55-83, was shown to exhibit ion-channel-like activity when reconstituted into (1) planar lipid bilayers and (2) lipid bilayers held at the tip of a glass pipette. The two set-ups led to differences in the oligomerization state of the peptide, which was rejected in differences in the conductance levels. Experiments under applied hydrostatic pressure affect the dynamics of the protein within the membrane.

Original language	English
Pages (from-to)	1089-1095
Number of pages	7
Journal	European Biophysics Journal
Volume	39
Issue number	7
DOIs	https://doi.org/10.1007/s00249-009-0518-x
State	Published - Jun 2010

Keywords

HIV-1
Membrane protein
Planar lipid bilayers
V

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1007/s00249-009-0518-x

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title = "Modulating the activity of the channel-forming segment of Vpr protein from HIV-1",

abstract = "Viral protein of regulation (Vpr) encoded by human immunodeficiency virus type 1 (HIV-1) is a short auxiliary protein that is 96 amino acids in length. During the viral life cycle, Vpr is released into the blood serum and is able to enter cellular membranes of noninfected cells. In this study a short peptide, Vpr55-83, was shown to exhibit ion-channel-like activity when reconstituted into (1) planar lipid bilayers and (2) lipid bilayers held at the tip of a glass pipette. The two set-ups led to differences in the oligomerization state of the peptide, which was rejected in differences in the conductance levels. Experiments under applied hydrostatic pressure affect the dynamics of the protein within the membrane.",

keywords = "HIV-1, Membrane protein, Planar lipid bilayers, V",

author = "Chen, {Chin Pei} and Clemens Kremer and Peter Henklein and Ulrich Schubert and Fink, {Rainer H.A.} and Fischer, {Wolfgang B.}",

note = "Funding Information: Acknowledgments WBF thanks the NYMU and the government of Taiwan for Wnancial support (Aim of Excellence Program). This work was supported by the National Science Council of Taiwan (NSC) and a Taiwanese–German scholarship to C.C. C.C. also acknowledges a DAAD fellowship.",

year = "2010",

month = jun,

doi = "10.1007/s00249-009-0518-x",

language = "English",

volume = "39",

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T1 - Modulating the activity of the channel-forming segment of Vpr protein from HIV-1

AU - Chen, Chin Pei

AU - Kremer, Clemens

AU - Henklein, Peter

AU - Schubert, Ulrich

AU - Fink, Rainer H.A.

AU - Fischer, Wolfgang B.

N1 - Funding Information: Acknowledgments WBF thanks the NYMU and the government of Taiwan for Wnancial support (Aim of Excellence Program). This work was supported by the National Science Council of Taiwan (NSC) and a Taiwanese–German scholarship to C.C. C.C. also acknowledges a DAAD fellowship.

PY - 2010/6

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N2 - Viral protein of regulation (Vpr) encoded by human immunodeficiency virus type 1 (HIV-1) is a short auxiliary protein that is 96 amino acids in length. During the viral life cycle, Vpr is released into the blood serum and is able to enter cellular membranes of noninfected cells. In this study a short peptide, Vpr55-83, was shown to exhibit ion-channel-like activity when reconstituted into (1) planar lipid bilayers and (2) lipid bilayers held at the tip of a glass pipette. The two set-ups led to differences in the oligomerization state of the peptide, which was rejected in differences in the conductance levels. Experiments under applied hydrostatic pressure affect the dynamics of the protein within the membrane.

AB - Viral protein of regulation (Vpr) encoded by human immunodeficiency virus type 1 (HIV-1) is a short auxiliary protein that is 96 amino acids in length. During the viral life cycle, Vpr is released into the blood serum and is able to enter cellular membranes of noninfected cells. In this study a short peptide, Vpr55-83, was shown to exhibit ion-channel-like activity when reconstituted into (1) planar lipid bilayers and (2) lipid bilayers held at the tip of a glass pipette. The two set-ups led to differences in the oligomerization state of the peptide, which was rejected in differences in the conductance levels. Experiments under applied hydrostatic pressure affect the dynamics of the protein within the membrane.

KW - HIV-1

KW - Membrane protein

KW - Planar lipid bilayers

KW - V

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DO - 10.1007/s00249-009-0518-x

M3 - Article

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SN - 0175-7571

VL - 39

SP - 1089

EP - 1095

JO - European Biophysics Journal

JF - European Biophysics Journal

IS - 7

ER -

Modulating the activity of the channel-forming segment of Vpr protein from HIV-1

Abstract

Keywords

UN SDGs

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