pubmed-article:20688520 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20688520 | lifeskim:mentions | umls-concept:C0042776 | lld:lifeskim |
pubmed-article:20688520 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
pubmed-article:20688520 | lifeskim:mentions | umls-concept:C1155265 | lld:lifeskim |
pubmed-article:20688520 | lifeskim:mentions | umls-concept:C1412831 | lld:lifeskim |
pubmed-article:20688520 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
pubmed-article:20688520 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
pubmed-article:20688520 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
pubmed-article:20688520 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
pubmed-article:20688520 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:20688520 | pubmed:dateCreated | 2010-8-31 | lld:pubmed |
pubmed-article:20688520 | pubmed:abstractText | The interferon-inducible, transmembrane protein BST-2 (CD317, tetherin) directly holds fully formed enveloped virus particles to the cells that produce them, inhibiting their spread. BST-2 inhibits members of the retrovirus, filovirus, arenavirus and herpesvirus families. These viruses encode a variety of proteins to degrade BST-2 and/or direct it away from its site of action at the cell surface. Viral antagonism has subjected BST-2 to positive selection, leading to species-specific differences that presented a barrier to the transmission of simian immunodeficiency viruses (SIVs) to humans. This barrier was crossed by HIV-1 when its Vpu protein acquired activity as a BST-2 antagonist. Here, we review this new host-pathogen relationship and discuss its impact on the evolution of primate lentiviruses and the origins of the HIV pandemic. | lld:pubmed |
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pubmed-article:20688520 | pubmed:language | eng | lld:pubmed |
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pubmed-article:20688520 | pubmed:citationSubset | IM | lld:pubmed |
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