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Bolduan, S.* ; Hubel, P.* ; Reif, T.* ; Lodermeyer, V.* ; Höhne, K. ; Fritz, J.V.* ; Sauter, D.* ; Kirchhoff, F.* ; Fackler, O.T.* ; Schindler, M. ; Schubert, U.*

HIV-1 Vpu affects the anterograde transport and the glycosylation pattern of NTB-A.

Virology 440, 190-203 (2013)
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HIV-1 Vpu induces downregulation of cell surface NTB-A to evade lysis of HIV-1 infected cells by NK cells. Here we show that Vpu affects the anterograde transport and the glycosylation pattern of NTB-A by a mechanism that is distinct from the Vpu induced downregulation of CD4 and tetherin. In the presence of Vpu, only the high mannose form of NTB-A was detectable, suggesting that Vpu prevented the formation of the mature form of NTB-A. This phenomenon is associated with the ability of Vpu to downregulate cell surface NTB-A by retention of NTB-A within the Golgi-compartment. Furthermore, the Vpu-mediated effect on NTB-A glycosylation is highly conserved among Vpu proteins derived from HIV-1 and SIV and corresponds to the level of downregulation of NTB-A. Together, these results suggest that the reduction of NTB-A from the cell surface is associated with the Vpu-mediated effect on the glycosylation pattern of newly synthesized NTB-A molecules.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Vpu ; Ntb-a ; Slamf6 ; Hiv-1 ; Siv ; Pulse-chase ; N-linked Glycosylation ; Tetherin; Virus Type-1 Vpu ; Natural-killer-cells ; Ion-channel Activity ; Down-modulation ; Membrane-protein ; Endoplasmic-reticulum ; Hiv-1-infected Cells ; Transmembrane Domain ; Cytoplasmic Domain ; Secretory Pathway
ISSN (print) / ISBN 0042-6822
e-ISSN 0042-6822
Zeitschrift Virology
Quellenangaben Band: 440, Heft: 2, Seiten: 190-203 Artikelnummer: , Supplement: ,
Verlag Elsevier
Begutachtungsstatus Peer reviewed