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Ion Channel Activity of Vpu Proteins Is Conserved throughout Evolution of HIV-1 and SIV.

Greiner, Timo and Bolduan, Sebastian and Hertel, Brigitte and Groß, Christine and Hamacher, Kay and Schubert, Ulrich and Moroni, Anna and Thiel, Gerhard (2016):
Ion Channel Activity of Vpu Proteins Is Conserved throughout Evolution of HIV-1 and SIV.
In: Viruses, p. 325, 8, (12), ISSN 1999-4915,
[Article]

Abstract

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.

Item Type: Article
Erschienen: 2016
Creators: Greiner, Timo and Bolduan, Sebastian and Hertel, Brigitte and Groß, Christine and Hamacher, Kay and Schubert, Ulrich and Moroni, Anna and Thiel, Gerhard
Title: Ion Channel Activity of Vpu Proteins Is Conserved throughout Evolution of HIV-1 and SIV.
Language: English
Abstract:

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.

Journal or Publication Title: Viruses
Volume: 8
Number: 12
Divisions: 10 Department of Biology
10 Department of Biology > Plant Membrane Biophysics
10 Department of Biology > Computational Biology and Simulation
Date Deposited: 04 Jan 2017 11:09
Identification Number: pmid:27916968
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