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

Bolduan S, Reif T, Schindler M, Schubert U (2014)

Publication Type: Journal article

Publication year: 2014

Journal

Virology Elsevier

Publisher: Elsevier

Book Volume: 464-465

Pages Range: 375-84

DOI: 10.1016/j.virol.2014.07.034

Abstract

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 ?-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.

Authors with CRIS profile

Sebastian Bolduan Professur für Virologie Ulrich Schubert Professur für Virologie

Involved external institutions

Helmholtz Zentrum München - Deutsches Forschungszentrum für Gesundheit und Umwelt (HMGU) / Helmholtz Munich DE Germany (DE)

How to cite

APA:

Bolduan, S., Reif, T., Schindler, M., & Schubert, U. (2014). HIV-1 Vpu mediated downregulation of CD155 requires alanine residues 10, 14 and 18 of the transmembrane domain. Virology, 464-465, 375-84. https://dx.doi.org/10.1016/j.virol.2014.07.034

MLA:

Bolduan, Sebastian, et al. "HIV-1 Vpu mediated downregulation of CD155 requires alanine residues 10, 14 and 18 of the transmembrane domain." Virology 464-465 (2014): 375-84.

BibTeX: Download