Characterization of Thioredoxin System from Leptospira interrogans

N. SASONI; A.M. REINOSO; D.G. ARIAS; A.A. IGLESIAS; S.A. GUERRERO

Mendoza

Congreso; XLVIII Reunión Anual de la SAIB; 2012

SAIB

During tismc invasion, Lepto,~pirain termganv (the causative agentof Icptospirrmis) is cxposcd cd clnatcd ainounts of cxogcnousreactwe oxygen and nitrogen species, which are h~ghlyto xic for thebacteria. IIowever, this pathogen is able to mtablish a penistentintection in its human host. The rnehbolic palhwayb for redoxhomeorstasis in thisorganism are poorly understood. In this work, weprcscl~l Ihe cluhg. ~ecuwbi~mxetx ptessiori and CwicLiuualcharacterizatim or he fhioredoxin system (lhiuredoxin, TRX andIhioredoxin reductase. TRXR) from L. in fernguns. The LirrTRXR(a low molecular mass TRXR) was evaluated in itsability b catal ysethe NAUPH dependent reduction of DTNB and LinTRX. LinTKXsys&m cuuld be assayed as a Cmctiunal =dux pair Lhak iugethe~with 7Cys typical panxiredoxin (Lin2CysPn;) mediates theNhDPH-dependent reduction of hydroperoxides. Moreover.Lin2CysPrx was able to accept elcctms from betcrologousthioredoxin systemand itwas shown to bcsmsitive to ovemxidafionhy peroxide ~ubmrateT. his work srmngIy supports the occurrence ofTRX system in I, iratemuguns, adding valuc m the genome pmjec?information of this pathogen.Granted by PIP 112 2008--01-02519, PPIC 07 668 and PICT´OB1754.