Envelope Deglycosylation Enhances Antigenicity of HIV-1 gp41 Epitopes for Both Broad Neutralizing Antibodies and Their Unmutated Ancestor Antibodies 英文参考文献.docVIP

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Envelope Deglycosylation Enhances Antigenicity of HIV-1 gp41 Epitopes for Both Broad Neutralizing Antibodies and Their Unmutated Ancestor Antibodies 英文参考文献.doc

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Envelope Deglycosylation Enhances Antigenicity of HIV-1 gp41 Epitopes for Both Broad Neutralizing Antibodies and Their Unmutated Ancestor Antibodies 英文参考文献

EnvelopeDeglycosylationEnhancesAntigenicityofHIV- 1gp41EpitopesforBothBroadNeutralizingAntibodies andTheirUnmutatedAncestorAntibodies Ben-JiangMa1,S.MunirAlam1,2,EdenP.Go3,XiaozhiLu1,HeatherDesaire3,GeorgiaD.Tomaras1,4,5, CindyBowman1,LauraL.Sutherland1,RichardM.Scearce1,SampaSantra7,NormanL.Letvin7, ThomasB.Kepler6,Hua-XinLiao1,2.*,BartonF.Haynes1,2,4. * 1Duke Human Vaccine Institute, Duke University School of Medicine, Durham, North Carolina, United States of America, 2Department of Medicine, Duke University School of Medicine, Durham, North Carolina, United States ofAmerica, 3Department ofChemistry, University ofKansas, Lawrence, Kansas, United States of America, 4DepartmentofImmunology,DukeUniversitySchoolofMedicine,Durham,NorthCarolina,UnitedStatesofAmerica,5DeparmentofSurgery,DukeUniversitySchoolof Medicine, Durham, North Carolina, United States of America, 6Center for Computational Immunology, Duke University School of Medicine, Durham, North Carolina, UnitedStatesofAmerica,7BethIsraelDeaconessMedicalCenter,HarvardMedicalSchool,Boston,Massachusetts,UnitedStatesofAmerica Abstract The HIV-1 gp41 envelope (Env) membrane proximal external region (MPER) is an important vaccine target that in rare subjectscanelicitneutralizingantibodies.OnemechanismproposedforrarityofMPERneutralizingantibodygenerationis lack of reverted unmutated ancestor (putative naive B cell receptor) antibody reactivity with HIV-1 envelope. We have studiedtheeffectofpartialdeglycosylationundernon-denaturing(native)conditionsongp140EnvantigenicityforMPER neutralizingantibodiesandtheirrevertedunmutatedancestorantibodies.WefoundthatnativedeglycosylationofcladeB JRFL gp140 as well as group M consensus gp140 Env CON-S selectively increased the reactivity of Env with the broad neutralizinghumanmAbs,2F5and4E10.Whereasfullyglycosylatedgp140Enveitherdidnotbind(JRFL),orweaklybound (CON-S),2F5and4E10revertedunmutatedancestors,nativelydeglycosylatedJRFLandCON-Sgp140Envsdidbindwellto theseputativemimicsof