Tetherin

Bone marrow stromal cell antigen 2
Rendering based on PDB 2X7A.
Available structures PDB 2X7A, 2XG7, 3MQ7, 3MQ9, 3MQB, 3MQC, 3NWH
Identifiers
Symbols	BST2; CD317; TETHERIN
External IDs	OMIM: 600534 MGI: 1916800 HomoloGene: 48277 GeneCards: BST2 Gene
Gene Ontology Molecular function • signal transducer activity • protein homodimerization activity Cellular component • late endosome • Golgi apparatus • integral to plasma membrane • anchored to membrane • plasma membrane part Biological process • humoral immune response • signal transduction • cell-cell signaling • multicellular organismal development • cell proliferation • B cell activation • positive regulation of I-kappaB kinase/NF-kappaB cascade • innate immune response • defense response to virus Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	684	69550
Ensembl	ENSG00000130303	ENSMUSG00000046718
UniProt	Q10589	Q8R2Q8
RefSeq (mRNA)	NM_004335	NM_198095.2
RefSeq (protein)	NP_004326	NP_932763.1
Location (UCSC)	Chr 19: 17.5 – 17.52 Mb	Chr 8: 74.06 – 74.06 Mb
PubMed search	[1]	[2]

Tetherin also known as bone marrow stromal antigen 2 is a protein that in humans is encoded by the BST2 gene. In addition, tetherin has been designated as CD317 (cluster of differentiation 317).

Function

Tetherin is a human cellular protein which inhibits retrovirus infection by preventing the diffusion of virus particles after budding from infected cells. 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 viruses such as the Lassa and Marburg virions suggesting a common mechanism that inhibits enveloped virus release without interaction with viral proteins.

Structure

Tetherin is a type 2 integral membrane protein, with the N-terminus in the cytoplasm, one membrane spanning domain, and a C-terminus modified by the addition of a glycosyl-phosphatidylinositol (gpi) anchor. When the virion buds from the surface of the cell, one of the tetherin membrane domains is in the new viral membrane, the other remains in the plasma membrane, tethering the virion to the cell. It is antagonized by the viral protein Vpu which is thought to work by targeting tetherin for degradation via the β-TrCP2 dependent pathway.

Tetherin exists as a dimer on the surface of cells, and prevention of dimerisation by mutating the cystine residues, prevents tetherin from inhibiting virus release, although it is still detectable in the cell.

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Furuya Y, Takasawa S, Yonekura H, et al. (1996). "Cloning of a cDNA encoding rat bone marrow stromal cell antigen 1 (BST-1) from the islets of Langerhans.". Gene 165 (2): 329–30. doi:10.1016/0378-1119(95)00540-M. PMID 8522202. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Ohtomo T, Sugamata Y, Ozaki Y, et al. (1999). "Molecular cloning and characterization of a surface antigen preferentially overexpressed on multiple myeloma cells.". Biochem. Biophys. Res. Commun. 258 (3): 583–91. doi:10.1006/bbrc.1999.0683. PMID 10329429. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Matsuda A, Suzuki Y, Honda G, et al. (2003). "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways.". Oncogene 22 (21): 3307–18. doi:10.1038/sj.onc.1206406. PMID 12761501. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Vidal-Laliena M, Romero X, March S, et al. (2006). "Characterization of antibodies submitted to the B cell section of the 8th Human Leukocyte Differentiation Antigens Workshop by flow cytometry and immunohistochemistry.". Cell. Immunol. 236 (1-2): 6–16. doi:10.1016/j.cellimm.2005.08.002. PMID 16157322. 
• Elortza F, Mohammed S, Bunkenborg J, et al. (2006). "Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment.". J. Proteome Res. 5 (4): 935–43. doi:10.1021/pr050419u. PMID 16602701. 

External links

• MeSH BST2+protein,+human

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