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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 8:325 (2016)
Verlagsversion Forschungsdaten DOI
Open Access Gold
Creative Commons Lizenzvertrag
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Viroporin ; Virus Channel Evolution ; Vpu Channel Function ; Vpu Transmembrane Domain; Human Macrophages; Membrane-protein; Immunodeficiency; Release; Cells; Phosphorylation; Identification; Degradation; Retrovirus; Mechanism
ISSN (print) / ISBN 1999-4915
e-ISSN 1999-4915
Zeitschrift Viruses
Quellenangaben Band: 8, Heft: 12, Seiten: , Artikelnummer: 325 Supplement: ,
Verlag MDPI
Verlagsort Basel
Begutachtungsstatus Peer reviewed