Role of Oxidative Stress on SARS-CoV (SARS) and SARS-CoV-2 (COVID-19) Infection: A Review

Abstract

Novel coronavirus disease 2019 (COVID-19) has resulted in a global pandemic and is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Several studies have suggested that a precise disulfide-thiol balance is crucial for viral entry and fusion into the host cell and that oxidative stress generated from free radicals can affect this balance. Here, we reviewed the current knowledge about the role of oxidative stress on SARS-CoV and SARS-CoV-2 infections. We focused on the impact of antioxidants, like NADPH and glutathione, and redox proteins, such as thioredoxin and protein disulfide isomerase, that maintain the disulfide-thiol balance in the cell. The possible influence of these biomolecules on the binding of viral protein with the host cell angiotensin-converting enzyme II receptor protein as well as on the severity of COVID-19 infection was discussed.

Keywords: Angiotensin-converting enzyme 2; COVID-19; Oxidative stress; SARS; SARS-CoV2; Spike protein.

Fig. 1

Structure of SARS-CoV virion

Fig. 2

Structures of protein complexes of a SARS-CoV⋯ACE2 (PDB: 3D0G) and b SARS-CoV-2⋯ACE2 (PDB: 6M0J). ACE2 shown in gray and spike glycoprotein in blue. Both visualized using New Cartoon drawing method. All the disulfide bridges between cysteine residues are shown in golden vdW spheres and thiol groups in magenta licorice (Color figure online)

Fig. 3

Renin angiotensin system. ACE angiotensin-converting enzyme

Fig. 4

NADPH/NADP⁺ equilibrium and ROS. Glucose 6-phosphate dehydrogenase is an important enzyme in the regeneration of NADPH but was not a focus of this review