COVID-19: Invades Erythrocytes through Plasmodium Falciparum Antigen and Complement-Like System (preprint)

Abstract

Malaria symptoms are very similar to those of COVID-19, and infections can be symptomatic or asymptomatic. Common immunodominant epitopes are shared by the SARS-CoV-2 proteins and the Plasmodium falciparum antigen. Through bioinformatics methods such as domain search, this study discovered that the S, ORF3a proteins contained Plasmodium antigens rich in tryptophan and threonine. ORF3a, ORF8, S, and N and others also had more extended autotransporter domains. The Plasmodium antigen of S protein contained a C1q domain capable of binding to the complement receptor 1 on the red blood cell membrane. ORF3a contained the Plasmodium antigen EBA-175 domain, which was capable of binding to glycophorin A on the red blood cell membrane. S and ORF3a were bound to band 4.1 to anchor on the erythrocyte membrane skeleton, respectively. The Membrane attack complex component of the S protein formed fusion pores on the red blood cell membrane. Then it injected viral genetic material into the mature red blood cell. ORF3a used a thiol-activated cytolysin domain to create hemolytic pores in the red blood cell membrane. The coagulation factor calcium ions were involved in the red blood cell invasion process. The invasion would have no discernible hemolysis or hypoxia reactions. According to the Plasmodium antigen type for SARS-COV-2, the blood cells of people with blood types A and Knops were susceptible to attack by SARS-COV-2 virus proteins.