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Figure 1 | Retrovirology

Figure 1

From: The formation of cysteine-linked dimers of BST-2/tetherin is important for inhibition of HIV-1 virus release but not for sensitivity to Vpu

Figure 1

Schematic of the BST-2 structure. (A) BST-2 is a type 2 integral membrane protein. The N-terminus localizes to the cytoplasm. The BST-2 ectodomain contains three cysteine residues (C53, C63, C91) and two potential sites for N-linked glycosylation (N65, N92). The C-terminus of BST-2 is modified by the addition of a glycosyl-phosphatidylinositol (gpi) anchor. (B) Predicted amino acid sequence of human BST-2. The predicted transmembrane region is indicated by a box. Signals for N-linked glycosylation are marked in blue; cysteine residues in the BST-2 extracellular domain are highlighted in yellow. The arrow points to the predicted site of cleavage for the addition of the gpi anchor [31].

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Retrovirology

ISSN: 1742-4690

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