KINETIC AND STRUCTURAL CHARACTERIZATION OF A TYPICAL 2-CYSTEINE PEROXIREDOXIN FROM Leptospira interrogans EXHIBITING REDOX SENSITIVITY

ARIAS DIEGO G.; REINOSO ANAHI; SASONI NATALIA; HARTMAN MATÍAS; IGLESIAS ALBERTO A.; GUERRERO SERGIO ADRIÁN

FREE RADICAL BIOLOGY AND MEDICINE

ELSEVIER SCIENCE INC

Lugar: Amsterdam; Año: 2014 vol. 77 p. 30 - 40

0891-5849

Little is known about the mechanisms by which Leptospira interrogans, the causativeagent of leptospirosis, copes with oxidative stress at the time it establishes persistentinfection within its human host. We report the molecular cloning of a gene encoding a2-Cys peroxiredoxin (LinAhpC) from this bacterium. After bioinformatic analysis wefound that LinAhpC contains the characteristic GGIG and YF motifs present inperoxiredoxins that are sensitive to over-oxidation (mainly eukaryotic proteins). Thesemotifs are absent in insensitive prokaryotic enzymes. Recombinant LinAhpC showedactive as thioredoxin peroxidase with sensitivity to over-oxidation by H2O2 (Chyp 1% ~30mM at pH 7.0 and 30 °C). So far, Anabaena 2-Cys peroxiredoxin, Helicobacter pyloriAhpC and LinAhpC are the only prokaryotic enzymes studied with these characteristics.The properties determined for LinAhpC suggest that the protein could be critical for theantioxidant defense capacity in L. interrogans.