HCV NS5A Protein Containing Potential Ligands for Both Src Homology 2 and 3 Domains Enhances Autophosphorylation of Src Family Kinase Fyn in B Cells 英文参考文献.docVIP

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HCV NS5A Protein Containing Potential Ligands for Both Src Homology 2 and 3 Domains Enhances Autophosphorylation of Src Family Kinase Fyn in B Cells 英文参考文献.doc

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HCV NS5A Protein Containing Potential Ligands for Both Src Homology 2 and 3 Domains Enhances Autophosphorylation of Src Family Kinase Fyn in B Cells 英文参考文献

HCVNS5AProteinContainingPotentialLigandsforBoth SrcHomology2and3DomainsEnhances AutophosphorylationofSrcFamilyKinaseFyninBCells KenjiNakashima1,KenjiTakeuchi1,2,KazuyasuChihara1,2,TomokoHoriguchi1,XuedongSun1, LinDeng3,IkuoShoji3,HakHotta3,KiyonaoSada1,2* 1DivisionofGenomeScienceandMicrobiology,DepartmentofPathologicalSciences,SchoolofMedicine,FacultyofMedicalSciences,UniversityofFukui,Eiheiji,Japan, 2Organization for Life Science Advancement Programs, University of Fukui, Eiheiji, Japan, 3Division of Microbiology, Center for Infectious Diseases, Kobe University GraduateSchoolofMedicine,Kobe,Japan Abstract HepatitisCvirus(HCV)infectsBlymphocytesandinducesmixedcryoglobulinemiaandBcellnon-Hodgkin’slymphoma.The molecular mechanism for the pathogenesis of HCV infection-mediated B cell disorders remains obscure. To identify the possibleroleforHCVnonstructural5A(NS5A)proteininBcells,wegeneratedthestableBcelllinesexpressingMyc-His taggedNS5A.Immunoprecipitationstudyinthepresenceorabsenceofpervanadate(PV)impliedthatNS5Awastyrosine phosphorylatedbypervanadate(PV)treatmentofthecells.Thereforeweexaminedpull-downassaybyusingglutathioneS- transferase(GST)-fusionproteinsofvariousSrchomology2(SH2)domains,whichassociateswithphosphotyrosinewithina specificaminoacidsequence.TheresultsshowedthatNS5AspecificallyboundtoSH2domainofFynfromPV-treatedB cellsinadditiontoSrchomology3(SH3)domain.SubstitutionofArg176 toLysintheSH2domainofFynabrogatedthis interaction.DeletionmutationalanalysisdemonstratedthatN-terminalregionofNS5Awasnotrequiredfortheinteraction withtheSH2domainofFyn.Tyr334wasidentifiedasatyrosinephosphorylationsiteinNS5A.Far-westernanalysisrevealed thatSH2domainofFyndirectlyboundtoNS5A.FynandNS5Awerecolocalizedinthelipidraft.Theseresultssuggestthat NS5AdirectlybindstotheSH2domainofFyninatyrosinephosphorylation-dependentmanner.Lastly,weshowedthatthe expression of NS5A in B cells increased phosphorylation of activation loop tyrosine in the kinase domain of Fyn. NS5A contai