Regulation of C-C chemokine receptor 5 (CCR5) stability by Lys¹⁹⁷ and by transmembrane protein aptamers that target it for lysosomal degradation.

ABSTRACT: C-C motif chemokine receptor 5 (CCR5) is a cell surface-associated, immune-regulatory G protein-coupled receptor (GCPR) with seven transmembrane helices. We previously reported the isolation and initial characterization of short artificial transmembrane protein aptamers, named "traptamers," that specifically down-regulate CCR5 expression and inhibit infection of human T cells by HIV strains that use CCR5 as a co-receptor. Here, we investigated the mechanism of traptamer-mediated CCR5 down-regulation and show that most of the traptamers (designated class 1 traptamers) form a stable complex with CCR5 and target it for lysosome-mediated degradation. The ability of these traptamers to down-regulate CCR5 depended on Lys¹⁹⁷ in the fifth transmembrane helix of CCR5. In the absence of t

SUBMITTER: Petti LM 

PROVIDER: S-EPMC5995508 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature