Biological and Medicinal Chemistry

COVID-19 Disease: ORF8 and Surface Glycoprotein Inhibit Heme Metabolism by Binding to Porphyrin



The novel coronavirus pneumonia (COVID-19) is an infectious acute respiratory infection caused by the novel coronavirus. The virus is a positive-strand RNA virus with high homology to bat coronavirus. Due to the limits of the existing experimental tools, many protein roles of novel coronavirus including ORF8 are still unclear. Therefore, in the current scene of an emergency epidemic, it is of high scientific significance to predict the biological role of viral proteins through bioinformatics methods. In this study, conserved domain analysis, homology modeling, and molecular docking were used to compare the biological roles of certain proteins of the novel coronavirus. The results showed the ORF8 and surface glycoprotein could bind to the porphyrin, respectively, while orf1ab, ORF10 and ORF3a proteins could coordinately attack heme to dissociate the iron to form the porphyrin. The mechanism seriously interfered with the normal heme anabolic pathway of the human body, being expected to result in human disease. According to the validation analysis of these finds, Chloroquine could prevent orf1ab, ORF3a and ORF10 to attack the heme to form the porphyrin, and inhibit the binding of ORF8 and surface glycoproteins to porphyrins to a certain extent. Therefore, this research is of high value to contemporary biological experiments, disease prevention and clinical treatment.

Version notes

1.Discussion part: The FRET characteristics of the porphyrin may be the primary survival mode on which the original virus relied.Therefore, we could believe that the novel coronavirus originated from an ancient virus that may have evolved over countless generations in bats. 2. keywords:novel coronavirus; orf1ab; chloroquine; blood; hemoglobin; diabetic; fluorescence resonance energy transfer; virus origin;


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