Molecular identification of a thioredoxin peroxidase in Babesia gibsoni with potential against oxidative stress.

ABSTRACT: Babesia gibsoni is the infectious agent of canine babesiosis, a vector-borne infection that poses a global threat to the canine health. As B. gibsoni is an erythrocytic intracellular parasite, the completion of its genome and transcriptome sequencing and analysis facilitates the elucidation of the mechanism of B. gibsoni residue in the erythrocyte. The main function of red blood cells (RBCs) is oxygen delivery; thus, B. gibsoni may be exposed to high levels of oxidative stress. To date, no report is available on the mechanism by which B. gibsoni survives oxidative stress inside the RBCs. In this study, the thioredoxin peroxidase, an important type of peroxidoxin, was identified from B. gibsoni, with 255 amino acids and a molecular weight of 27.7 kDa. There are two conserved "VCP" domains a

SUBMITTER: Guo J 

PROVIDER: S-EPMC11882686 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature