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Figure 3 | Retrovirology

Figure 3

From: Modulation of HIV-1-host interaction: role of the Vpu accessory protein

Figure 3

Schematic representations of Tetherin. Secondary and tertiary model of human Tetherin. Glycosylation sites at position 65 and 92 are shown as well as the GPI-anchor and the cytoplasmic, transmembrane (TM) and extracellular coiled-coil domains. The functional parallel dimeric state is shown here. (B) Tetherin topology. An amino-acid sequence alignment of human, chimpanzee, rhesus and African green monkey (agm) Tetherin alleles is shown below. Hyphens and bold letters represent respectively deletions and residues in human Tetherin under positive selection. Putative Ub-acceptor residues, cysteine residues involved in dimerization as well as N-glycosylation sites are labelled in orange, pink and red, respectively. Putative trafficking signals, the predicted transmembrane domain and the coiled-coil domain are highlighted in blue, green and yellow. The sites of interaction mapped for SIV Nef and HIV-1 Vpu are boxed in dark blue and dark green, respectively. Note that the SIV Nef-interacting region is deleted in human Tetherin. The site of cleavage prior to addition of the GPI lipid anchor is represented by the dashed line.

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