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@ARTICLE{Vasudevan:830254,
      author       = {Vasudevan, Ananda Ayyappan Jaguva and Hofmann, Henning and
                      Willbold, Dieter and Häussinger, Dieter and König, Bernd
                      and Münk, Carsten},
      title        = {{E}nhancing the {C}atalytic {D}eamination {A}ctivity of
                      {APOBEC}3{C} {I}s {I}nsufficient to {I}nhibit
                      {V}if-{D}eficient {HIV}-1},
      journal      = {Journal of molecular biology},
      volume       = {429},
      number       = {8},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2017-03827},
      pages        = {1171–1191},
      year         = {2017},
      abstract     = {The retroviral restriction factors of the APOBEC3 (A3)
                      cytidine deaminase family catalyze the deamination of
                      cytidines in single-stranded viral DNA. APOBEC3C (A3C) is a
                      strong antiviral factor against viral infectivity factor
                      (vif)-deficient simian immunodeficiency virus Δvif, which
                      is, however, a weak inhibitor against human immunodeficiency
                      virus (HIV)-1 for reasons unknown. The precise link between
                      the antiretroviral effect of A3C and its catalytic activity
                      is incompletely understood. Here, we show that the S61P
                      mutation in human A3C (A3C.S61P) boosted hypermutation in
                      the viral genomes of simian immunodeficiency virus Δvif and
                      murine leukemia virus but not in human immunodeficiency
                      virus HIV-1Δvif. The enhanced antiviral activity of
                      A3C.S61P correlated with enhanced in vitro cytidine
                      deamination. Furthermore, the S61P mutation did not change
                      the substrate specificity of A3C, ribonucleoprotein complex
                      formation, self-association, Zinc coordination, or viral
                      incorporation features. We propose that local structural
                      changes induced by the serine-to-proline substitution are
                      responsible for the gain of catalytic activity of A3C.S61P.
                      Our results are a first step toward an understanding of
                      A3C's DNA binding capacity, deamination-dependent editing,
                      and antiviral functions at the molecular level. We conclude
                      that the enhanced enzymatic activity of A3C is insufficient
                      to restrict HIV-1, indicating an unknown escape mechanism of
                      HIV-1.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000400720100006},
      pubmed       = {pmid:28315663},
      doi          = {10.1016/j.jmb.2017.03.015},
      url          = {https://juser.fz-juelich.de/record/830254},
}