Requirement of the CXXC Motif of Novel Francisella Infectivity Potentiator Protein B FipB, and FipA in Virulence of F. tularensis subsp. tularensis 英文参考文献.docVIP

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Requirement of the CXXC Motif of Novel Francisella Infectivity Potentiator Protein B FipB, and FipA in Virulence of F. tularensis subsp. tularensis 英文参考文献.doc

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Requirement of the CXXC Motif of Novel Francisella Infectivity Potentiator Protein B FipB, and FipA in Virulence of F. tularensis subsp. tularensis 英文参考文献

RequirementoftheCXXCMotifofNovelFrancisella InfectivityPotentiatorProteinBFipB,andFipAin VirulenceofF.tularensissubsp.tularensis AipingQin1,3,DavidW.Scott1,MeaghanM.Rabideau1,EmilyA.Moore1,BarbaraJ.Mann1,2* 1DepartmentofMedicine,UniversityofVirginia,Charlottesville,Virginia,UnitedStatesofAmerica,2DepartmentofMicrobiology,UniversityofVirginia,Charlottesville, Virginia,UnitedStatesofAmerica,3OfficeofLaboratoryManagement,ChineseCenterforDiseaseControlandPrevention,Beijing,PeoplesRepublicofChina Abstract ThelipoproteinencodedbytheFrancisellatularensissubsp.tularensislocusFTT1103isessentialforvirulence;anFTT1103 deletionmutantisdefectiveinuptakeandintracellularsurvival,andmicesurvivehighdosechallengesofgreaterthan108 bacteria.Thisproteinhastwoconserveddomains;oneisfoundinaclassofvirulenceproteinscalledmacrophageinfectivity potentiator(Mip)proteins,andtheotherinoxidoreductaseDisulfideBondformationproteinA(DsbA)-relatedproteins.We havedesignatedtheproteinencodedbyFTT1103asFipBforFrancisellainfectivitypotentiatorproteinB.ThelocusFTT1102 (fipA),whichisupstreamoffipB,alsohassimilaritytosameconservedMipdomain.Deletionandsite-specificmutantsoffipA and fipB were constructed in the Schu S4 strain, and characterized with respect to intracellular replication and in vivo virulence. A nonpolar fipA mutant demonstrated reduced survival in host cells, but was only slightly attenuated in vivo. AlthoughFipBproteinwaspresentinafipAmutant,theabundanceofthethreeisoformsofFipBwasaltered,suggesting thatFipAhasaroleinpost-translationalmodificationofFipB.SimilartomanyDsbAhomologues,FipBcontainsacysteine- anyaminoacid-anyaminoacid-cysteine(CXXC)motif.ThismotifwasfoundtobeimportantforFipB’sroleinvirulence;a deletionmutantcomplementedwithageneencodingaFipBproteininwhichthefirstcysteinewaschangedtoanalanine residue (AXXC) failed to restore intracellular survival or in vivo virulence. Complementation with a gene that encoded a CXXAcontainingFipBproteinwassignificantlydefectiveinintracellulargrowth