Abstract:
:Vif is essential for HIV-1 replication in T cells and macrophages. Vif recruits a host ubiquitin ligase complex to promote proteasomal degradation of the APOBEC3 restriction factors by poly-ubiquitination. The cellular transcription cofactor CBFβ is required for Vif function by stabilizing the Vif protein and promoting recruitment of a cellular Cullin5-RING ubiquitin ligase complex. Interaction between Vif and CBFβ is a promising therapeutic target, but little is known about the interfacial residues. We now demonstrate that Vif conserved residues E88/W89 are crucial for CBFβ binding. Substitution of E88/W89 to alanines impaired binding to CBFβ, degradation of APOBEC3, and virus infectivity in the presence of APOBEC3 in single-cycle infection. In spreading infection, NL4-3 with Vif E88A/W89A mutation replicated comparably to wild-type virus in permissive CEM-SS cells, but not in multiple APOBEC3 expressing non-permissive CEM cells. These results support a model in which HIV-1 Vif residues E88/W89 may participate in binding CBFβ.
journal_name
Virologyjournal_title
Virologyauthors
Matsui Y,Shindo K,Nagata K,Io K,Tada K,Iwai F,Kobayashi M,Kadowaki N,Harris RS,Takaori-Kondo Adoi
10.1016/j.virol.2013.11.004subject
Has Abstractpub_date
2014-01-20 00:00:00pages
82-7eissn
0042-6822issn
1096-0341pii
S0042-6822(13)00617-Xjournal_volume
449pub_type
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