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HIV-1 capsid is involved in post-nuclear entry steps.

Abstract：

BACKGROUND:HIV-1 capsid influences viral uncoating and nuclear import. Some capsid is detected in the nucleus but it is unclear if it has any function. We reported that the antibiotic Coumermycin-A1 (C-A1) inhibits HIV-1 integration and that a capsid mutation confers resistance to C-A1, suggesting that capsid might affect post-nuclear entry steps. RESULTS:Here we report that C-A1 inhibits HIV-1 integration in a capsid-dependent way. Using molecular docking, we identify an extended binding pocket delimited by two adjacent capsid monomers where C-A1 is predicted to bind. Isothermal titration calorimetry confirmed that C-A1 binds to hexameric capsid. Cyclosporine washout assays in Jurkat CD4+ T cells expressing engineered human TRIMCyp showed that C-A1 causes faster and greater escape from TRIMCyp restriction. Sub-cellular fractionation showed that small amounts of capsid accumulated in the nuclei of infected cells and C-A1 reduced the nuclear capsid. A105S and N74D capsid mutant viruses did not accumulate capsid in the nucleus, irrespective of C-A1 treatment. Depletion of Nup153, a nucleoporin located at the nuclear side of the nuclear pore that binds to HIV-1 capsid, made the virus less susceptible to TRIMCyp restriction, suggesting that Nup153 may help maintain some integrity of the viral core in the nucleus. Furthermore C-A1 increased binding of CPSF6, a nuclear protein, to capsid. CONCLUSIONS:Our results indicate that capsid is involved in post-nuclear entry steps preceding integration.

journal_name

Retrovirology

journal_title

Retrovirology

authors

Chen NY,Zhou L,Gane PJ,Opp S,Ball NJ,Nicastro G,Zufferey M,Buffone C,Luban J,Selwood D,Diaz-Griffero F,Taylor I,Fassati A

doi

10.1186/s12977-016-0262-0

subject

Has Abstract

pub_date

2016-04-23 00:00:00

pages

28

issn

1742-4690

pii

10.1186/s12977-016-0262-0

journal_volume

13

pub_type

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