Thioredoxin system in Listeria monocytogenes

Abstract:

Listeria monocytogenes is an important foodborne pathogenic microorganism. Its oxidative stress tolerance is the key ability to survive and mediate pathogenesis. Increasing of intracellular Reactive Oxygen Species (ROS) leads to imbalance of redox homeostasis, oxidative stress, and further damage of proteins as well as other large biological molecules. Cysteine and sulfur-containing amino acid of proteins are especially sensitive to ROS, and formation of disulfide bonds is an oxidation reaction, with two electrons removed from cysteine residues, which contributes to stabilizing protein structures and preventing protein damages. Antioxidant repair usually refers to the oxidation reaction of cysteine residues, consisting of disulfide bonds formation and breaking. Thioredoxin (Trx) family, including thioredoxin, glutaredoxin, and Dsb-like system, is a widely-distributed system responsible for oxidation repair in microorganisms. Here, we review the most recent research development of the Trx family from bacterial species and present our opinions of this family in L. monocytogenes, to better understand the regulatory network of Listeria during environmental adaption and host infection.