%0 Journal Article %1 citeulike:4544533 %A Perkovic, Mario %A Schmidt, Stanislaw %A Marino, Daniela %A Russell, Rebecca A. %A Stauch, Benjamin %A Hofmann, Henning %A Kopietz, Ferdinand %A Kloke, Bjorn-Philipp %A Zielonka, Jorg %A Strover, Heike %A Hermle, Johannes %A Lindemann, Dirk %A Pathak, Vinay K. %A Schneider, Gisbert %A Lochelt, Martin %A Cichutek, Klaus %A Munk, Carsten %D 2009 %J J. Biol. Chem. %K imported %N 9 %P 5819--5826 %R 10.1074/jbc.M808853200 %T Species-specific Inhibition of APOBEC3C by the Prototype Foamy Virus Protein Bet %U http://dx.doi.org/10.1074/jbc.M808853200 %V 284 %X The APOBEC3 cytidine deaminases are part of the intrinsic defense of cells against retroviruses. Lentiviruses and spumaviruses have evolved essential accessory proteins, Vif and Bet, respectively, which counteract the APOBEC3 proteins. We show here that Bet of the Prototype foamy virus inhibits the antiviral APOBEC3C activity by a mechanism distinct to Vif: Bet forms a complex with APOBEC3C without inducing its degradation. Bet abolished APOBEC3C dimerization as shown by coimmunoprecipitation and cross-linking experiments. These findings implicate a physical interaction between Bet and the APOBEC3C. Subsequently, we identified the Bet interaction domain in human APOBEC3C in the predicted APOBEC3C dimerization site. Taken together, these data support the hypothesis that Bet inhibits incorporation of APOBEC3Cs into retroviral particles. Bet likely achieves this by trapping APOBEC3C protein in complexes rendering them unavailable for newly generated viruses due to direct immobilization. 10.1074/jbc.M808853200

@article{citeulike:4544533, abstract = {The APOBEC3 cytidine deaminases are part of the intrinsic defense of cells against retroviruses. Lentiviruses and spumaviruses have evolved essential accessory proteins, Vif and Bet, respectively, which counteract the APOBEC3 proteins. We show here that Bet of the Prototype foamy virus inhibits the antiviral APOBEC3C activity by a mechanism distinct to Vif: Bet forms a complex with APOBEC3C without inducing its degradation. Bet abolished APOBEC3C dimerization as shown by coimmunoprecipitation and cross-linking experiments. These findings implicate a physical interaction between Bet and the APOBEC3C. Subsequently, we identified the Bet interaction domain in human APOBEC3C in the predicted APOBEC3C dimerization site. Taken together, these data support the hypothesis that Bet inhibits incorporation of APOBEC3Cs into retroviral particles. Bet likely achieves this by trapping APOBEC3C protein in complexes rendering them unavailable for newly generated viruses due to direct immobilization. 10.1074/jbc.M808853200}, added-at = {2009-05-19T18:00:18.000+0200}, author = {Perkovic, Mario and Schmidt, Stanislaw and Marino, Daniela and Russell, Rebecca A. and Stauch, Benjamin and Hofmann, Henning and Kopietz, Ferdinand and Kloke, Bjorn-Philipp and Zielonka, Jorg and Strover, Heike and Hermle, Johannes and Lindemann, Dirk and Pathak, Vinay K. and Schneider, Gisbert and Lochelt, Martin and Cichutek, Klaus and Munk, Carsten}, biburl = {https://www.bibsonomy.org/bibtex/2cf6b27ad73ee117650acfef178d3d1df/earthfare}, citeulike-article-id = {4544533}, description = {CiteULike: Everyone's library}, doi = {10.1074/jbc.M808853200}, interhash = {0cb8e442b851e7bd1c45979cc3f0cf8e}, intrahash = {cf6b27ad73ee117650acfef178d3d1df}, journal = {J. Biol. Chem.}, keywords = {imported}, month = {February}, number = 9, pages = {5819--5826}, posted-at = {2009-05-19 09:07:14}, priority = {2}, timestamp = {2009-05-19T18:03:27.000+0200}, title = {Species-specific Inhibition of APOBEC3C by the Prototype Foamy Virus Protein Bet}, url = {http://dx.doi.org/10.1074/jbc.M808853200}, volume = 284, year = 2009 }