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Abstract
The novel coronavirus pneumonia is a contagious acute respiratory disease caused by the SARS-COV-2 coronavirus. The pathogenic mechanism of the novel coronavirus is unknown, which presents a significant impediment to the patient rescue. A conserved domain search strategy was utilized in this work to determine that a large number of viral proteins could bind to hemoglobin. S could bind to extracellular hemoglobin. SARS-COV-2 virus proteins interacted with porphyrins. SARS-COV-2 viruses could synthesize heme from porphobilinogen and encode all the similar enzymes required for the process. Both E and ORF3a contained heme-binding sites. ORF3a's Arg134 and E's Cys44 were the heme-iron binding sites, respectively. ORF3a also contained homologous domains to human cytochrome C reductase and bacterial EFeB protein. The molecular docking analysis revealed that ORF3a and ORF8 proteins were shown to be capable of attacking hemoglobin's 1-beta chain, whereas ORF3a was found to be effective in capturing heme for dissociation to iron and porphyrin. Deoxyhemoglobin was more susceptible to viral attack than oxidized hemoglobin. In summary, the combination of viral proteins to porphyrins and their metal compounds would improve the ability to permeate cell membranes and generate oxygen free radicals (ROS). It may be associated with viral infections and epidemic transmission. Viral proteins regulated the production and function of NO, CO and CO2 by inhibiting the activity of hemoglobin, thereby affecting immune cell function. Viral proteins' attack on hemoglobin could result in symptoms such as respiratory distress and blood clotting, damage to numerous organs and tissues, and disruption of normal human heme metabolism.
Version notes
1. Background:
ADD:
1). The relationship between porphyrin （and heme） and virus
2). Calculation results show how SARS-COV-2 virus protein is secreted into the serum and invaded red blood cells
2. Method:
1). Delete the molecular docking between HEME and viral protein
3. Results:
ADD:
1). The SARS-COV-2 virus protein binds porphyrin and produces heme.
2). SARS-COV-2 virus protein bound to hemoglobin
3). Heme binding motif of SARS-COV-2 virus protein
4). SARS-COV-2 ORF8 attacks hemoglobin
5). SARS-COV-2 ORF3a attacks cytochrome C mutants, cytochrome P450 mutants, myoglobin mutants
Delete:
1). the molecular docking between HEME and viral proteins
2). N protein heme domain search result
3). Molecular docking between SARS-COV-2 virus protein and compound drugs
4. Discussion
1). Delete the description of the secretion of SARS-COV-2 virus protein and the way of attacking hemoglobin. (Already stated in the background)
2). Rewrite the SARS-COV-2 virus carcinogenicity statement
Content
