Our collaborative study with the Zhang Lab was published in the Journal of Virology ("Truncated CPSF6 Forms Higher-Order Complexes that Bind and Disrupt HIV-1 Capsid") showing that a truncated form of the host protein CPSF6 (CPSF6-358) oligomerizes around HIV-1 capsid and is associated with more rapid core uncoating. This truncated protein sequesters HIV DNA in the cytoplasm of cells.
In the video below that Zhou made, CPSF6-358 (green) expressed in cells associates with viral complexes (red) and then separate, suggesting that oligomerization of CPSF6-358 around capsid leads to dissociation of the core.
If the capsid does not bind to CPSF6-358 either due to mutations (e.g. N74D, A77V) or treatment with a small molecule inhibitor (i.e. PF74), oligomerization did not occur. Doug showed with our capsid permeabilization assay that HIV capsid opens more rapidly in cells expressing CPSF6-358 than cells not expressing it:
The Zhang lab showed similar results in vitro using CA tubes.
Read the paper here: http://jvi.asm.org/content/92/13/e00368-18.long
Nice imaging work Zhou and Doug!
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