COVID-19:Attacks the 1-Beta Chain of Hemoglobin and Captures the Porphyrin to Inhibit Human Heme Metabolism

Abstract

The novel coronavirus pneumonia (COVID-19) is an infectious acute respiratory caused by the novel coronavirus. The virus is a positive-strand RNA virus with high homology to bat coronavirus. In this study, conserved domain analysis, homology modeling, and molecular docking were used to compare the biological roles of specific proteins of the novel coronavirus. The results showed that some viral structural and nonstructural proteins could bind to the porphyrin, respectively. At the same time, orf1ab, ORF10 and ORF3a proteins coordinated to attack heme on the 1-beta chain of hemoglobin, dissociating iron to form porphyrin. Deoxyhemoglobin is more vulnerable to virus attacks than oxidized hemoglobin. The attack will cause less and less hemoglobin that can carry oxygen and carbon dioxide, producing symptoms of respiratory distress. Virus attack damaged many organs and tissues. Lung cells are toxic and inflammatory due to derivatives produced by the attack, which eventually resulted in ground-glass-like lung images. Capillaries easily broken due to inflammation. Proteins such as fibrinogen filled the capillaries' cracks through the coagulation reaction. Therefore, many fibrin and thrombus gathered in the lung tissue of critically ill patients. The mechanism also interfered with the normal heme anabolic pathway of the human body, expecting to result in human disease. This paper is only for academic discussion, the correctness of the theory needs to be confirmed by other experiments. According to the reader's suggestion, the content of the drug-related efficacy analysis has been deleted. Due to the side effects of drugs, please consult a qualified doctor for detailed treatment information, and do not take the drug yourself. We look forward to these discoveries bringing more ideas to people and inspiring people's confidence in defeating the virus.