Binding of the Heterogeneous Ribonucleoprotein K (hnRNP K) to the Epstein-Barr Virus Nuclear Antigen 2 (EBNA2) Enhances Viral LMP2A Expression 英文参考文献.docVIP

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Binding of the Heterogeneous Ribonucleoprotein K (hnRNP K) to the Epstein-Barr Virus Nuclear Antigen 2 (EBNA2) Enhances Viral LMP2A Expression 英文参考文献.doc

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Binding of the Heterogeneous Ribonucleoprotein K (hnRNP K) to the Epstein-Barr Virus Nuclear Antigen 2 (EBNA2) Enhances Viral LMP2A Expression 英文参考文献

BindingoftheHeterogeneousRibonucleoproteinK (hnRNPK)totheEpstein-BarrVirusNuclearAntigen2 (EBNA2)EnhancesViralLMP2AExpression HenrikGross1,ChristineHennard2,IliasMasouris2,ChristianCassel1,StephanieBarth1,UteStober- Gra¨sser1,AlfredoMamiani1,BodoMoritz3,DirkOstareck4,AntjeOstareck-Lederer4,NilsNeuenkirchen5, UtzFischer5,WenDeng6,HeinrichLeonhardt6,ElfriedeNoessner2,ElisabethKremmer2, FriedrichA.Gra¨sser1* 1Institute of Virology, Saarland University Medical School, Homburg/Saar, Germany, 2Institute of Molecular Immunology, Helmholtz Zentrum Mu¨nchen, German Research Center for Environmental Health, Munich, Germany, 3Institute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, Halle (Saale), Germany,4ExperimentalResearchUnit,DepartmentofIntensiveCareandIntermediateCare,UniversityHospitalAachen,RWTHAachenUniversity,Aachen,Germany, 5Department ofBiochemistry, Biocenter of the University of Wu¨rzburg, Wu¨rzburg, Germany, 6Department of Biology, Center for Integrated Protein Science Munich, LudwigMaximiliansUniversityMunich,Planegg-Martinsried,Germany Abstract TheEpstein-BarrVirus(EBV)-encodedEBNA2protein,whichisessentialfortheinvitrotransformationofB-lymphocytes, interferes with cellular processes by binding to proteins via conserved sequence motifs. Its Arginine-Glycine (RG) repeat elementcontainseithersymmetricallyorasymmetricallydi-methylatedarginineresidues(SDMAandADMA,respectively). EBNA2bindsviaitsSDMA-modifiedRG-repeattothesurvivalmotorneuronsprotein(SMN)andviatheADMA-RG-repeatto theNP9proteinofthehumanendogenousretrovirusK(HERV-K(HML-2)Type1).Thehypothesisofthisworkwasthatthe methylatedRG-repeatmimicsanepitopesharedwithcellularproteinsthatisusedforinteractionwithtargetstructures. WithmonoclonalantibodiesagainstthemodifiedRG-repeat,weindeedidentifiedcellularhomologuesthatapparentlyhave thesamesurfacestructureasmethylatedEBNA2.WiththeSDMA-specificantibodies,weprecipitatedtheSmproteinD3 (SmD3) which, like EBNA2, binds via its SDMA-modifi