Abstract：
:The chemokine receptor CCR7 plays a crucial role in the homing of central memory and naive T cells to peripheral lymphoid organs. Here, we show that the HIV-1 accessory protein Vpu downregulates CCR7 on the surface of CD4(+) T cells. Vpu and CCR7 were found to specifically interact and colocalize within the trans-Golgi network, where CCR7 is retained. Downmodulation of CCR7 did not involve degradation or endocytosis and was strictly dependent on Vpu expression. Stimulation of HIV-1-infected primary CD4(+) T cells with the CCR7 ligand CCL19 resulted in reduced mobilization of Ca(2+), reduced phosphorylation of Erk1/2, and impaired migration toward CCL19. Specific amino acid residues within the transmembrane domain of Vpu that were previously shown to be critical for BST-2 downmodulation (A14, A18, and W22) were also necessary for CCR7 downregulation. These results suggest that BST-2 and CCR7 may be downregulated via similar mechanisms.
journal_name
Cell Repjournal_title
Cell reportsauthors
Ramirez PW,Famiglietti M,Sowrirajan B,DePaula-Silva AB,Rodesch C,Barker E,Bosque A,Planelles Vdoi
10.1016/j.celrep.2014.05.015subject
Has Abstractpub_date
2014-06-26 00:00:00pages
2019-30issue
6issn
2211-1247pii
S2211-1247(14)00390-8journal_volume
7pub_type
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