PuSH - Publication Server of Helmholtz Zentrum München

Bolduan, S. ; Reif, T.* ; Schindler, M. ; Schubert, U.*

HIV-1 Vpu mediated downregulation of CD155 requires alanine residues 10, 14 and 18 of the transmembrane domain.

Virology 464-465, 375-384 (2014)
Open Access Green as soon as Postprint is submitted to ZB.
HIV-1 NL4-3 Vpu induces downregulation of cell surface CD155, a ligand for the DNAM-1 activating receptor of NK and CD8(+) T cells, to evade NK cell mediated immune response. Here we show that the conserved alanine residues at positions 10, 14 and 18 in the TM domain of Vpu are required for the efficient downregulation of cell surface CD155. In contrast, the CK-2 phosphorylation sites and the second α-helix in the cytoplasmic Vpu domain have no influence on the surface expression of CD155. Thus, compared to Vpu׳s effect on CD4, NTB-A and tetherin, the Vpu mediated downregulation of CD155 is an independent Vpu function. We finally show that in contrast to other lentiviral strains, only Vpu and Nef from HIV-1 M NL4-3 potently interfere with CD155 surface expression. Thus, Vpu seems to subvert NK cell responses against HIV-1 infected T cells by modulation of receptors necessary for NK cell activation.
Additional Metrics?
Edit extra informations Login
Publication type Article: Journal article
Document type Scientific Article
Keywords Cd155 ; Hiv-1 ; Nef ; Siv ; Vpu; Virus Type-1 Vpu; Natural-killer-cells; T-cells; Endoplasmic-reticulum; Ntb-a; Protein; Tetherin; Nef; Modulation; Release
ISSN (print) / ISBN 0042-6822
e-ISSN 0042-6822
Journal Virology
Quellenangaben Volume: 464-465, Issue: 1, Pages: 375-384 Article Number: , Supplement: ,
Publisher Elsevier
Publishing Place San Diego
Reviewing status Peer reviewed