The Full Wiki

More info on Tetherin

Tetherin: Wikis


Note: Many of our articles have direct quotes from sources you can cite, within the Wikipedia article! This article doesn't yet, but we're working on it! See more info or our list of citable articles.


From Wikipedia, the free encyclopedia

Bone marrow stromal cell antigen 2
Symbols BST2; Tetherin; ‎CD317
External IDs OMIM600534 MGI1916800 HomoloGene48277 GeneCards: BST2 Gene
RNA expression pattern
PBB GE BST2 201641 at tn.png
More reference expression data
Species Human Mouse
Entrez 684 69550
Ensembl ENSG00000130303 ENSMUSG00000046718
UniProt Q10589 Q8R2Q8
RefSeq (mRNA) NM_004335 NM_198095
RefSeq (protein) NP_004326 NP_932763
Location (UCSC) Chr 19:
17.37 - 17.38 Mb
Chr 8:
74.46 - 74.47 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.[1][2] In addition tetherin has been designated as CD317 (cluster of differentiation 317).



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.[3][4] suggesting a common mechanism that inhibits enveloped virus release without interaction with viral proteins.


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.[5] 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[6] which is thought to work by targetting tetherin for degredation via the β-TrCP2 dependent pathway.[7]

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.[8]


  1. ^ Ishikawa J, Kaisho T, Tomizawa H, Lee BO, Kobune Y, Inazawa J, Oritani K, Itoh M, Ochi T, Ishihara K, et al. (Aug 1995). "Molecular cloning and chromosomal mapping of a bone marrow stromal cell surface gene, BST2, that may be involved in pre-B-cell growth". Genomics 26 (3): 527-34. PMID 7607676.  
  2. ^ "Entrez Gene: BST2 bone marrow stromal cell antigen 2".  
  3. ^ Sakuma T, Noda T, Urata S, Kawaoka Y, Yasuda J (March 2009). "Inhibition of Lassa and Marburg virus production by tetherin". J. Virol. 83 (5): 2382–5. doi:10.1128/JVI.01607-08. PMID 19091864.  
  4. ^ Thaczuk D (2008-02-11). "Tetherin: a newly discovered host cell protein that inhibits HIV replication". NAM AIDS Map.  
  5. ^ Andrew AJ, Miyagi E, Kao S, Strebel K (2009). "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". Retrovirology 6: 80. doi:10.1186/1742-4690-6-80. PMID 19737401.  
  6. ^ Neil SJ, Zang T, Bieniasz PD (January 2008). "Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu". Nature 451 (7177): 425–30. doi:10.1038/nature06553. PMID 18200009.  
  7. ^ Mangeat B, Gers-Huber G, Lehmann M, Zufferey M, Luban J, Piguet V (September 2009). "HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation". PLoS Pathog. 5 (9): e1000574. doi:10.1371/journal.ppat.1000574. PMID 19730691.  
  8. ^ Andrew AJ, Miyagi E, Kao S, Strebel K (2009). "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". Retrovirology 6: 80. doi:10.1186/1742-4690-6-80. PMID 19737401.  

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. PMID 12477932.  
  • 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. PMID 15489334.  
  • 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

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



Got something to say? Make a comment.
Your name
Your email address