A Novel Thioredoxin-Dependent Peroxiredoxin (TPx-Q) Plays an Important Role in Defense Against Oxidative Stress and Is a Possible Drug Target in Babesia microti.

ABSTRACT: Thioredoxin peroxidases (TPxs) are ubiquitous cysteine-based peroxidases that reduce peroxides as part of antioxidant defenses and redox signaling and are essential for Babesia microti protection against adverse environment agents like reactive oxygen species (ROS) and reactive nitrogen species (RNS). To better systematically understand TPxs, we identified a novel 2-Cys peroxiredoxin-Q (BmTPx-Q) of B. microti. The full-length BmTPx-Q gene is 653 bp that consists of an intact open reading frame of 594 bp that encodes a 197-amino acid protein. The predicted protein has a molecular weight of 22.3 kDa and an isoelectric point of 9.18. Moreover, BmTPx-Q showed low identity at the amino acid level to other peroxiredoxins (Prxs) among the currently known subfamilies. The recombinant

SUBMITTER: Zhang H 

PROVIDER: S-EPMC7040034 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature