Disulfide Bonds in the Ectodomain of Anthrax Toxin Receptor 2 Are Required for the Receptor-Bound Protective-Antigen Pore to Function 英文参考文献.docVIP

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Disulfide Bonds in the Ectodomain of Anthrax Toxin Receptor 2 Are Required for the Receptor-Bound Protective-Antigen Pore to Function 英文参考文献.doc

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Disulfide Bonds in the Ectodomain of Anthrax Toxin Receptor 2 Are Required for the Receptor-Bound Protective-Antigen Pore to Function 英文参考文献

DisulfideBondsintheEctodomainofAnthraxToxin Receptor2AreRequiredfortheReceptor-Bound Protective-AntigenPoretoFunction JianjunSun*¤,R.JohnCollier DepartmentofMicrobiologyandMolecularGenetics,HarvardMedicalSchool,Boston,Massachusetts,UnitedStatesofAmerica Abstract Background:Cell-surfacereceptorsplayessentialrolesinanthraxtoxinactionbyprovidingthetoxinwithahigh-affinity anchor and self-assembly site on the plasma membrane, mediating the toxin entry into cells through endocytosis, and shifting the pH threshold for prepore-to-pore conversion of anthrax toxin protective antigen (PA) to a more acidic pH, therebyinhibitingprematureporeformation.Eachofthetwoknownanthraxtoxinreceptors,ANTXR1andANTXR2,hasan ectodomaincomprisedofanN-terminalvonWillebrandfactorAdomain(VWA),whichbindsPA,andanuncharacterized immunoglobulin-likedomain(Ig)thatconnectsVWAtothemembrane-spanningdomain.PotentialrolesofthereceptorIg domaininanthraxtoxinactionhavenotbeeninvestigatedheretofore. Methodology/PrincipalFindings:WeexpressedandpurifiedtheANTXR2ectodomain(R2-VWA-Ig)inE.coliandshowed thatitcontainsthreedisulfidebonds:oneinR2-VWAandtwoinR2-Ig.Reductionoftheectodomaininhibitedfunctioning ofthepore,asmeasuredbyK releasefromliposomesorChinesehamsterovarycellsorbyPA-mediatedtranslocationofa + modelsubstrateacrosstheplasmamembrane.However,reductiondidnotaffectbindingoftheectodomaintoPAorthe transition of ectodomain-bound PA prepore to the pore conformation. The inhibitory effect depended specifically on reductionofthedisulfideswithinR2-Ig. Conclusions/Significance:WeconcludethatdisulfideintegritywithinR2-Igisessentialforproperfunctioningofreceptor- boundPApore.Thisfindingprovidesanovelvenuetoinvestigatethemechanismofanthraxtoxinactionandsuggestsnew strategiesforinhibitingtoxinaction. Citation:SunJ,CollierRJ(2010)DisulfideBondsintheEctodomainofAnthraxToxinReceptor2AreRequiredfortheReceptor-BoundProtective-AntigenPoreto Function.PLoSONE5(5):e10553.doi:10.1371/journal.pone.0010553 Editor:AdamJ.Ratner