Peroxiredoxins—The Underrated Actors during Virus-Induced Oxidative Stress

Abstract

Enhanced production of reactive oxygen species (ROS) triggered by various stimuli, including viral infections, has attributed much attention in the past years. It has been shown that different viruses that cause acute or chronic diseases induce oxidative stress in infected cells and dysregulate antioxidant its antioxidant capacity. However, most studies focused on catalase and superoxide dismutases, whereas a family of peroxiredoxins (Prdx), the most effective peroxide scavengers, were given little or no attention. In the current review, we demonstrate that peroxiredoxins scavenge hydrogen and organic peroxides at their physiological concentrations at various cell compartments, unlike many other antioxidant enzymes, and discuss their recycling. We also provide data on the regulation of their expression by various transcription factors, as they can be compared with the imprint of viruses on transcriptional machinery. Next, we discuss the involvement of peroxiredoxins in transferring signals from ROS on specific proteins by promoting the oxidation of target cysteine groups, as well as briefly demonstrate evidence of nonenzymatic, chaperone, functions of Prdx. Finally, we give an account of the current state of research of peroxiredoxins for various viruses. These data clearly show that Prdx have not been given proper attention despite all the achievements in general redox biology.

Transcriptome Analysis of Redox Systems and Polyamine Metabolic Pathway in Hepatoma and Non-Tumor Hepatocyte-like Cells

“…Next, we analyzed the levels of the expression of ROS-scavenging enzymes. These included superoxide dismutases (SOD), which are enzymes that catalyze the reaction of the disproportionation of the superoxide radical (O2•−) into molecular oxygen (O2) and hydrogen peroxide (H2O2); catalase (CAT), which decomposes hydrogen peroxide into water and molecular oxygen, is capable of oxidizing low molecular weight alcohols and nitrites in the presence of hydrogen peroxide; and glutathione peroxidases and peroxiredoxins, which catalyze the reduction of organic hydroperoxides to alcohols and hydrogen peroxide to water [ 38 , 39 , 40 , 41 ]. The families of superoxide dismutases, glutathione peroxidases, and peroxiredoxins are represented by three, eight, and six proteins, respectively.…”

“…The redox status of a cell is tightly regulated by thioredoxins (TXN) ang glutaredoxins (GLRX) and their reductases. These enzymes restore oxidized peroxiredoxins and glutathione peroxidases [ 39 , 42 ]. RNAseq analysis revealed that hepatocyte-like HepaRG cells show lower levels of the expression of TXN but higher levels of reductase (TXNRD1) and glutaredoxin (GLRX) ( Figure 3 a,b).…”

The landscape of potential health benefits of carotenoids as natural supportive therapeutics in protecting against Coronavirus infection

“…Superoxide dismutase (SOD) [131] , heme oxygenase-1 (HO-1) [90] , catalase (CAT) [154] , glutathione peroxidase (GPX) [243] , glutathione S-transferase (GST) [210] , peroxiredoxin (PrxI) [112] , and nuclear factor erythroid 2–related factor 2 (Nrf2) [55] are enzymes that mitigate oxidative stress and are implicated in the pathogenesis of COVID-19. The correlation between decreased expression of SOD3 in lungs and severity of COVID-19 has been reported in elderly patients [131] .…”

Plasma-Like Culture Medium for the Study of Viruses

“…Redox status of a host cell depends on rates of production of reactive oxygen species (ROS) and cellular antioxidant capacity. ROS scavenging is mainly achieved by two families of highly active peroxidases, peroxiredoxins and glutathione peroxidases, as they have high affinity to H 2 O 2 and organic peroxides ( 97 , 98 ). Neutralization of ROS leads to oxidation of these enzymes with subsequent recycling by thioredoxin or glutaredoxin systems.…”