Antimicrobial Activity and Molecular Mechanism of the CRES Protein 英文参考文献.docVIP

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Antimicrobial Activity and Molecular Mechanism of the CRES Protein 英文参考文献.doc

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Antimicrobial Activity and Molecular Mechanism of the CRES Protein 英文参考文献

AntimicrobialActivityandMolecularMechanismofthe CRESProtein LiWang1,2.,QingYuan1,2.,SunhongChen1,2,HengCai1,2,MeigeLu1,2,YueLiu1,2,ChenXu1,2 * 1DepartmentofHistologyandEmbryology,ShanghaiJiaotongUniversitySchoolofMedicine,Shanghai,China,2ShanghaiKeyLaboratoryofReproductiveMedicine, Shanghai,China Abstract Cystatin-related epididymal spermatogenic (CRES) protein, a member of the cystatin superfamily of cysteine protease inhibitors (also known as CST8), exhibits highly specific, age-dependent expression in mouse testis and epididymis. The CRES protein possesses four highly conserved cysteine residues which govern the overall conformation of the cystatins throughtheformationoftwodisulfidebonds.Previousstudieshaverevealedthatothercystatinfamilymembers,suchas cystatin3andcystatin11,showantibacterialactivityinvitro.Thispromptedustoinvestigatethepotentialantimicrobial activity of the CRES protein. Colony forming assays and spectrophotometry were used to investigate the effects of recombinantCRESproteinonEscherichiacoli(E.coli)andUreaplasmaurealyticum(Uu),respectively,invitro.Afterincubation ofE.coliwithCRESrecombinantproteinfusedwithglutathione-S-transferase(GST),asubstantialdecreaseincolonyforming unitswasobserved,andtheeffectwasdoseandtimedependent.Furthermore,ittooklongerforUutogrowtoplateau stagewhenincubatedwithGST-CRESrecombinantproteincomparedwiththecontrolGST.TheantibacterialandAnti-Uu activitieswerenotimpairedwhenthecysteine residuesofCRESproteinweremutated,indicatingthattheantimicrobial effectwasnotdependentonitsdisulfidebonds.FunctionalanalysisofthreeCRESpolypeptidesshowedthattheN-terminal 30residues(N30)hadnoantimicrobialactivitywhileN60showedsimilaractivityasfull-lengthCRESprotein.Theseresults suggest that the active center of CRES protein resides between amino acid residues 31 and 60 of its N-terminus. Mechanistically, E. coli membrane permeabilization was increased in a dose-dependent manner, and macromolecular synthesis was inhibited on treatment with