Enzymatic Shaving of the Tegument Surface of Live Schistosomes for Proteomic Analysis A Rational Approach to Select Vaccine Candidates 英文参考文献.docVIP

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Enzymatic Shaving of the Tegument Surface of Live Schistosomes for Proteomic Analysis A Rational Approach to Select Vaccine Candidates 英文参考文献.doc

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Enzymatic Shaving of the Tegument Surface of Live Schistosomes for Proteomic Analysis A Rational Approach to Select Vaccine Candidates 英文参考文献

EnzymaticShavingoftheTegumentSurfaceofLive SchistosomesforProteomicAnalysis:ARational ApproachtoSelectVaccineCandidates WilliamCastro-Borges1*¤,AdamDowle2,RachelS.Curwen1,JaneThomas-Oates3,R.AlanWilson1 1Department ofBiology, UniversityofYork, Heslington,York, UnitedKingdom,2Department ofBiology andCentreofExcellence inMassSpectrometry,Technology Facility,UniversityofYork,Heslington,York,UnitedKingdom,3DepartmentofChemistryandCentreofExcellenceinMassSpectrometry,UniversityofYork,Heslington, York,UnitedKingdom Abstract Background: The membrane-associated and membrane-spanning constituents of the Schistosoma mansoni tegument surface, the parasite’s principal interface with the host bloodstream, have recently been characterized using proteomic techniques. Biotinylation of live worms using membrane-impermeant probes revealed that only a small subset of the proteins was accessible to the reagents. Their position within the multilayered architecture of the surface has not been ascertained. Methodology/PrincipalFindings:Anenzymaticshavingapproachonlivewormshasnowbeenusedtoreleasethemost accessible components, for analysis by MS/MS. Treatment with trypsin, or phosphatidylinositol-specific phospholipase C (PiPLC),onlyminimally impairedmembrane integrity.PiPLC-enriched proteins weredistinguishedfromthosereleasedin parasitevomitusorbyhandlingdamage,usingisobarictagging.Trypsinreleasedfivemembraneproteins,Sm200,Sm25 andthreeannexins,plushostCD44andthecomplementfactorsC3andC4.Nutrienttransportersandionchannelswere absent from the trypsin fraction, suggesting a deeper location in the surface complex; surprisingly, two BAR-domain containing proteinswerereleased. Sevenparasite andtwohostproteins wereenrichedby PiPLCtreatment,thevaccine candidate Sm29 being the most prominent along with two orthologues of human CD59, potentially inhibitors of complementfixation.TheenzymescarbonicanhydraseandAPD-ribosylcyclasewerealsoenriched,plusSm200andalkaline phosphatase. Host GPI-anch