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Ion channel activity of Vpu proteins is conserved throughout evolution of HIV-1 and SIV.
Viruses 8:325 (2016)
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.
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3.042
1.016
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6
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Viroporin ; Virus Channel Evolution ; Vpu Channel Function ; Vpu Transmembrane Domain; Human Macrophages; Membrane-protein; Immunodeficiency; Release; Cells; Phosphorylation; Identification; Degradation; Retrovirus; Mechanism
Language
Publication Year
2016
HGF-reported in Year
2016
ISSN (print) / ISBN
1999-4915
e-ISSN
1999-4915
Journal
Viruses
Quellenangaben
Volume: 8,
Issue: 12,
Article Number: 325
Publisher
MDPI
Publishing Place
Basel
Reviewing status
Peer reviewed
Institute(s)
Institute of Virology (VIRO)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Immune Response and Infection
PSP Element(s)
G-502700-006
PubMed ID
27916968
DOI
10.3390/v8120325
WOS ID
WOS:000392484600005
Scopus ID
85007072384
Erfassungsdatum
2016-12-31