Ion Channel Activity of Vpu Proteins Is Conserved throughout Evolution of HIV-1 and SIV
The human immunodeficiency virus type 1 (HIV-1) protein Vpu is encoded exclusively by HIV-1 and related simian immunodeficiency viruses (SIVs). The transmembrane domain of the protein has dual functions: it counteracts the human restriction factor tetherin and forms a cation channel. Since these two...
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doaj-ee7db4c86ef141ca8ac2849307e034e62020-11-24T22:13:52ZengMDPI AGViruses1999-49152016-12-0181232510.3390/v8120325v8120325Ion Channel Activity of Vpu Proteins Is Conserved throughout Evolution of HIV-1 and SIVTimo Greiner0Sebastian Bolduan1Brigitte Hertel2Christine Groß3Kay Hamacher4Ulrich Schubert5Anna Moroni6Gerhard Thiel7Membrane Biophysics, Technische Universität Darmstadt, 64287 Darmstadt, GermanyInstitute of Virology, Helmholtz Zentrum Munich, 85764 Oberschleißheim, GermanyMembrane Biophysics, Technische Universität Darmstadt, 64287 Darmstadt, GermanyComputational Biology & Simulation Group, Deparment of Biology, Technische Universität Darmstadt, 64287 Darmstadt, GermanyComputational Biology & Simulation Group, Deparment of Biology, Technische Universität Darmstadt, 64287 Darmstadt, GermanyInstitute of Virology, Friedrich Alexander University, 91054 Erlangen, GermanyDepartment of Biology and CNR IBF-Mi, Università degli Studi di Milano, 20122 Milano, ItalyMembrane Biophysics, Technische Universität Darmstadt, 64287 Darmstadt, GermanyThe human immunodeficiency virus type 1 (HIV-1) protein Vpu is encoded exclusively by HIV-1 and related simian immunodeficiency viruses (SIVs). The transmembrane domain of the protein has dual functions: it counteracts the human restriction factor tetherin and forms a cation channel. Since these two functions are causally unrelated it remains unclear whether the channel activity has any relevance for viral release and replication. Here we examine structure and function correlates of different Vpu homologs from HIV-1 and SIV to understand if ion channel activity is an evolutionary conserved property of Vpu proteins. An electrophysiological testing of Vpus from different HIV-1 groups (N and P) and SIVs from chimpanzees (SIVcpz), and greater spot-nosed monkeys (SIVgsn) showed that they all generate channel activity in HEK293T cells. This implies a robust and evolutionary conserved channel activity and suggests that cation conductance may also have a conserved functional significance.http://www.mdpi.com/1999-4915/8/12/325Vpu channel functionviroporinvirus channel evolutionVpu transmembrane domain |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Timo Greiner Sebastian Bolduan Brigitte Hertel Christine Groß Kay Hamacher Ulrich Schubert Anna Moroni Gerhard Thiel |
spellingShingle |
Timo Greiner Sebastian Bolduan Brigitte Hertel Christine Groß Kay Hamacher Ulrich Schubert Anna Moroni Gerhard Thiel Ion Channel Activity of Vpu Proteins Is Conserved throughout Evolution of HIV-1 and SIV Viruses Vpu channel function viroporin virus channel evolution Vpu transmembrane domain |
author_facet |
Timo Greiner Sebastian Bolduan Brigitte Hertel Christine Groß Kay Hamacher Ulrich Schubert Anna Moroni Gerhard Thiel |
author_sort |
Timo Greiner |
title |
Ion Channel Activity of Vpu Proteins Is Conserved throughout Evolution of HIV-1 and SIV |
title_short |
Ion Channel Activity of Vpu Proteins Is Conserved throughout Evolution of HIV-1 and SIV |
title_full |
Ion Channel Activity of Vpu Proteins Is Conserved throughout Evolution of HIV-1 and SIV |
title_fullStr |
Ion Channel Activity of Vpu Proteins Is Conserved throughout Evolution of HIV-1 and SIV |
title_full_unstemmed |
Ion Channel Activity of Vpu Proteins Is Conserved throughout Evolution of HIV-1 and SIV |
title_sort |
ion channel activity of vpu proteins is conserved throughout evolution of hiv-1 and siv |
publisher |
MDPI AG |
series |
Viruses |
issn |
1999-4915 |
publishDate |
2016-12-01 |
description |
The human immunodeficiency virus type 1 (HIV-1) protein Vpu is encoded exclusively by HIV-1 and related simian immunodeficiency viruses (SIVs). The transmembrane domain of the protein has dual functions: it counteracts the human restriction factor tetherin and forms a cation channel. Since these two functions are causally unrelated it remains unclear whether the channel activity has any relevance for viral release and replication. Here we examine structure and function correlates of different Vpu homologs from HIV-1 and SIV to understand if ion channel activity is an evolutionary conserved property of Vpu proteins. An electrophysiological testing of Vpus from different HIV-1 groups (N and P) and SIVs from chimpanzees (SIVcpz), and greater spot-nosed monkeys (SIVgsn) showed that they all generate channel activity in HEK293T cells. This implies a robust and evolutionary conserved channel activity and suggests that cation conductance may also have a conserved functional significance. |
topic |
Vpu channel function viroporin virus channel evolution Vpu transmembrane domain |
url |
http://www.mdpi.com/1999-4915/8/12/325 |
work_keys_str_mv |
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