Antioxidant Defense by Thioredoxin Can Occur Independently of Canonical Thiol-Disulfide Oxidoreductase Enzymatic Activity.
Cell Rep
; 14(12): 2901-11, 2016 Mar 29.
Article
in En
| MEDLINE
| ID: mdl-26997275
The thiol-disulfide oxidoreductase CXXC catalytic domain of thioredoxin contributes to antioxidant defense in phylogenetically diverse organisms. We find that although the oxidoreductase activity of thioredoxin-1 protects Salmonella enterica serovar Typhimurium from hydrogen peroxide in vitro, it does not appear to contribute to Salmonella's antioxidant defenses in vivo. Nonetheless, thioredoxin-1 defends Salmonella from oxidative stress resulting from NADPH phagocyte oxidase macrophage expression during the innate immune response in mice. Thioredoxin-1 binds to the flexible linker, which connects the receiver and effector domains of SsrB, thereby keeping this response regulator in the soluble fraction. Thioredoxin-1, independently of thiol-disulfide exchange, activates intracellular SPI2 gene transcription required for Salmonella resistance to both reactive species generated by NADPH phagocyte oxidase and oxygen-independent lysosomal host defenses. These findings suggest that the horizontally acquired virulence determinant SsrB is regulated post-translationally by ancestrally present thioredoxin.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Thioredoxins
/
Bacterial Proteins
/
Antioxidants
Type of study:
Prognostic_studies
Language:
En
Journal:
Cell Rep
Year:
2016
Document type:
Article
Affiliation country:
Estados Unidos
Country of publication:
Estados Unidos