2LK9, 2X7A, 2XG7, 3MQ7, 3MQ9, 3MQB, 3MQC, 3NWH, 4P6Z68469550ENSG00000130303ENSMUSG00000046718Q10589Q8R2Q8NM_004335NM_198095NP_004326NP_932763Tetherin, also known as bone marrow stromal antigen 2, is a lipid raft associated protein that in humans is encoded by the BST2 gene.

When the presence of virus and viral components is detected by recognition molecules such as (RIG-I), a cascades of interactions happen between signaling molecules, eventually the signal reaches the nucleus to upregulate the expression of interferon-stimulated genes (ISGs), this in turn activates IFN-α pathway to send the signal to neighboring cells, which causes upregulation in the expression of other ISGs and many viral restriction factors, such as tetherin.

Initially discovered as an inhibitor to HIV-1 infection in the absence of Vpu, tetherin has also been shown to inhibit the release of other RNA viruses such as the Lassa and Marburg virions[14][15] suggesting a common mechanism that inhibits enveloped virus release without interaction with viral proteins.

[19] Although Tetherin is localized to the lipid rafts on the surface of the cells, they are endocytosed to be sorted through TGN by clathrin-dependent pathway.

It is antagonized by the viral protein Vpu[20] which is thought to work by targeting tetherin for degradation via the β-TrCP2 dependent pathway.

Studies have shown that it is not the amino acid sequence, but the topology of tetherin is required for the tethering of virions on the cell surface.

VP35 of Ebola, inhibits multiple steps of IFN-signaling pathway, which blocks the induction of tetherin as a downstream effect.

[32] This article incorporates text from the United States National Library of Medicine, which is in the public domain.