Tetherin

Tetherin, also known as BST-2 (Bone Marrow Stromal Cell Antigen 2), CD317 or HIV-1 Vpu-sensitive factor is a protein that in humans is encoded by the BST2 gene. Tetherin is an interferon-inducible antiviral protein that has the unique ability to inhibit the release of certain enveloped viruses from infected cells.

Function

Tetherin is a type II transmembrane protein that is found on the surface of cells. It has been shown to have antiviral activity against a broad range of viruses. Tetherin achieves this by physically tethering budding virions to the membrane of the infected cell, preventing their release and spread.

Structure

Tetherin is a small protein with a molecular weight of approximately 30-36 kDa. It has a unique structure consisting of a short N-terminal cytoplasmic tail, a transmembrane domain, an extracellular coiled-coil domain, and a C-terminal GPI anchor. This structure allows it to span the lipid bilayer twice, with both the N and C termini located in the cytoplasm.

Role in Disease

Tetherin has been implicated in a number of diseases, most notably HIV infection. The HIV-1 accessory protein Vpu counteracts the antiviral activity of tetherin by targeting it for degradation and removing it from the site of viral budding. This allows the virus to spread and infect other cells. Tetherin's role in other viral infections, such as Ebola and Influenza, is currently being investigated.

Research

Research into tetherin is ongoing, with the aim of developing new antiviral therapies. Understanding how tetherin works and how viruses counteract its activity could lead to the development of drugs that enhance its antiviral function or prevent viruses from counteracting it.

See Also

• Antiviral protein
• HIV
• Ebola
• Influenza

References

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