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Viruses 2016, 8(12), 325; doi:10.3390/v8120325

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

1
Membrane Biophysics, Technische Universität Darmstadt, 64287 Darmstadt, Germany
2
Institute of Virology, Helmholtz Zentrum Munich, 85764 Oberschleißheim, Germany
3
Computational Biology & Simulation Group, Deparment of Biology, Technische Universität Darmstadt, 64287 Darmstadt, Germany
4
Institute of Virology, Friedrich Alexander University, 91054 Erlangen, Germany
5
Department of Biology and CNR IBF-Mi, Università degli Studi di Milano, 20122 Milano, Italy
These authors contributed equally to this work.
Current address: Department of Neuroscience, Physiology & Pharmacology, University College London, London WC1E 6BT, UK.
*
Author to whom correspondence should be addressed.
Academic Editor: Andrew Mehle
Received: 7 October 2016 / Revised: 14 November 2016 / Accepted: 22 November 2016 / Published: 1 December 2016
(This article belongs to the Section Animal Viruses)
View Full-Text   |   Download PDF [1677 KB, uploaded 6 December 2016]   |  

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. View Full-Text
Keywords: Vpu channel function; viroporin; virus channel evolution; Vpu transmembrane domain Vpu channel function; viroporin; virus channel evolution; Vpu transmembrane domain
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Greiner, T.; Bolduan, S.; Hertel, B.; Groß, C.; Hamacher, K.; Schubert, U.; Moroni, A.; Thiel, G. Ion Channel Activity of Vpu Proteins Is Conserved throughout Evolution of HIV-1 and SIV. Viruses 2016, 8, 325.

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