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dc.contributor.authorTsai-Yu, Linen_US
dc.contributor.authorEmerman, Michaelen_US
dc.date.accessioned2010-04-21T15:51:14Z
dc.date.available2010-04-21T15:51:14Z
dc.date.issued2006en_US
dc.identifier.citationLin T, Emerman M. Cyclophilin A interacts with diverse lentiviral capsids. Retrovirology. 2006;3(1):70.en_US
dc.identifier.other10.1186/1742-4690-3-70en_US
dc.identifier.urihttp://www.retrovirology.com/content/3/1/70en_US
dc.identifier.urihttp://hdl.handle.net/1773/15737
dc.description.abstractBackground: 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.sponsorshipThis work was supported by NIH grant R37 AI30937 to M.E.en_US
dc.language.isoen_USen_US
dc.titleCyclophilin A interacts with diverse lentiviral capsidsen_US
dc.typeArticleen_US


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