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@ARTICLE{Gu:841985,
      author       = {Gu, Qinyong and Zhang, Zeli and Gertzen, Christoph G. W.
                      and Häussinger, Dieter and Gohlke, Holger and Münk,
                      Carsten},
      title        = {{I}dentification of a {C}onserved {I}nterface of {H}uman
                      {I}mmunodeficiency {V}irus {T}ype 1 and {F}eline
                      {I}mmunodeficiency {V}irus {V}ifs with {C}ullin 5},
      journal      = {Journal of virology},
      volume       = {92},
      number       = {6},
      issn         = {1098-5514},
      address      = {Baltimore, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2018-00272},
      pages        = {e01697-17},
      year         = {2018},
      abstract     = {The apolipoprotein B mRNA-editing enzyme, catalytic
                      polypeptide-like (APOBEC3, A3) family of DNA cytidine
                      deaminases are intrinsic restriction factors against
                      retroviruses. In felids such as the domestic cat (Felis
                      catus), the APOBEC3 (A3) genes encode for the A3Z2s, A3Z3,
                      and A3Z2Z3 antiviral cytidine deaminases. Only A3Z3 and
                      A3Z2Z3 inhibit viral infectivity factor (Vif)-deficient
                      feline immunodeficiency virus (FIV). FIV Vif protein
                      interacts with Cullin (CUL), Elongin B (ELOB), and Elongin C
                      (ELOC) to form an E3 ubiquitination complex to induce the
                      degradation of feline A3s. However, the functional domains
                      in FIV Vif for interaction with Cullin are poorly
                      understood. Here, we found that the expression of
                      dominant-negative CUL5 prevented the degradation of feline
                      A3s by FIV Vif, while dominant-negative CUL2 had no
                      influence on the degradation of A3. In
                      co-immunoprecipitation assays, FIV Vif bound to CUL5 but not
                      CUL2. To identify the CUL5 interaction site in FIV Vif, the
                      conserved amino acids from position 47 to 160 of FIV Vif
                      were mutated, but these mutations did not impair the binding
                      of Vif to CUL5. By focusing on a potential zinc-binding
                      motif (K175— C161—C184—C187) of FIV Vif, we found a
                      conserved hydrophobic region (174IR175) that is important
                      for CUL5 interaction. Mutating this region also impaired the
                      FIV Vif-induced degradation of feline A3s. Based on a
                      structural model of the FIV Vif/CUL5 interaction, residues
                      52LW53 in CUL5 were identified as mediating the binding to
                      FIV Vif. By comparing our results to the HIV-1 Vif/CUL5
                      interaction surface (120IR121, a hydrophobic region that is
                      localized in the zinc-binding motif), we suggest that the
                      CUL5 interaction surface in the diverse HIV-1 and FIV Vif is
                      evolutionarily conserved indicating a strong structural
                      constraint. However, the FIV Vif/CUL5 interaction is
                      zinc-independent, which contrasts with the zinc-dependence
                      of HIV-1 Vif.},
      cin          = {JSC / NIC / ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406 /
                      I:(DE-Juel1)ICS-6-20110106},
      pnm          = {574 - Theory, modelling and simulation (POF3-574) / 553 -
                      Physical Basis of Diseases (POF3-553) / 511 - Computational
                      Science and Mathematical Methods (POF3-511)},
      pid          = {G:(DE-HGF)POF3-574 / G:(DE-HGF)POF3-553 /
                      G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29263270},
      UT           = {WOS:000427447100012},
      doi          = {10.1128/JVI.01697-17},
      url          = {https://juser.fz-juelich.de/record/841985},
}