Cyclophilin A interacts with diverse lentiviral capsids

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Cyclophilin A interacts with diverse lentiviral capsids

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dc.contributor.author Tsai-Yu, Lin en_US
dc.contributor.author Emerman, Michael en_US
dc.date.accessioned 2010-04-21T15:51:14Z
dc.date.available 2010-04-21T15:51:14Z
dc.date.issued 2006 en_US
dc.identifier.citation Lin T, Emerman M. Cyclophilin A interacts with diverse lentiviral capsids. Retrovirology. 2006;3(1):70. en_US
dc.identifier.other 10.1186/1742-4690-3-70 en_US
dc.identifier.uri http://www.retrovirology.com/content/3/1/70 en_US
dc.identifier.uri http://hdl.handle.net/1773/15737
dc.description.abstract Background: The capsid (CA) protein of HIV-1 binds with high affinity to the host protein cyclophilin A (CypA). This binding positively affects some early stage of the viral life-cycle because prevention of binding either by drugs that occupy that active site of cyclophilin A, by mutation in HIV-1 CA, or RNAi that knocks down intracellular CypA level diminishes viral infectivity. The closely related lentivirus, SIVcpz also binds CypA, but it was thought that this interaction was limited to the HIV-1/SIVcpz lineage because other retroviruses failed to interact with CypA in a yeast two-hybrid assay. Results: We find that diverse lentiviruses, FIV and SIVagmTAN also bind to CypA. Mutagenesis of FIV CA showed that an amino acid that is in a homologous position to the proline at amino acid 90 of HIV-1 CA is essential for FIV interactions with CypA. Conclusion: These results demonstrate that CypA binding to lentiviruses is more widespread than previously thought and suggest that this interaction is evolutionarily important for lentiviral infection. en_US
dc.description.sponsorship This work was supported by NIH grant R37 AI30937 to M.E. en_US
dc.language.iso en_US en_US
dc.title Cyclophilin A interacts with diverse lentiviral capsids en_US
dc.type Article en_US


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