AI Article Synopsis
- Chemiluminescence tests showed that SARS-CoV-2 N and S proteins can significantly suppress oxidation by reactive oxygen species (ROS) at different pH levels.
- Both viral proteins exhibited antioxidant capabilities, performing better than albumin in neutral environments and matching its effectiveness at physiological pH.
- These findings suggest that the viral proteins may not contribute to oxidative stress during infection, potentially serving as an evolutionary self-defense mechanism against host immune responses.
Article Abstract
Chemiluminescence was used to test the susceptibility of the SARS-CoV-2 N and S proteins to oxidation by reactive oxygen species (ROS) at pH 7.4 and pH 8.5. The Fenton's system generates various ROS (HO, OH, OH, OOH). All proteins were found to significantly suppress oxidation (the viral proteins exhibited 25-60% effect compared to albumin). In the second system, HO was used both as a strong oxidant and as a ROS. A similar effect was observed (30-70%); N protein approached the effect of albumin at physiological pH (∼45%). In the O-generation system, albumin was most effective in the suppression of generated radicals (75%, pH 7.4). The viral proteins were more susceptible to oxidation (inhibition effect no more than 20%, compared to albumin). The standard antioxidant assay confirmed the strong antioxidant capacity of both viral proteins (1.5-1.7 fold higher than albumin). These results demonstrate the effective and significant inhibition of ROS-induced oxidation by the proteins. Obviously, the viral proteins could not be involved in the oxidative stress reactions during the course of the infection. They even suppress the metabolites involved in its progression. These results can be explained by their structure. Probably, an evolutionary self-defense mechanism of the virus has been developed.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10050197 | PMC |
| http://dx.doi.org/10.1016/j.ab.2023.115137 | DOI Listing |
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