We speculated that the lipopolysaccharide synthesized by the SARS-COV-2 virus protein made the SARS-COV-2 virus more effectively attached to the ACE2 receptor on the host cell surface. The interaction significantly increases viral infectivity and promotes hypercytokineemia. More lipopolysaccharides activated monocytes and phagocytes to release many inflammatory factors, destroyed adipose tissue and vascular endothelial tissue, and induced diabetes and high blood pressure. Cells infected by the SARS-COV-2 virus often used cell surface polysaccharides to build expanded barriers to prevent their host's defense mechanisms. Lipopolysaccharide enhanced the ability of infected cells to resist T cells, NK cells, and drugs. For cells infected with the SARS-COV-2 virus, similar drug resistance problems would also arise because of the ABC transport function of ORF7a protein. Figure . Extracellular ORF7a (PDB ID: 7ci3; 14-96) binds LPS and CD14. A. the BPI1/LBP domain of extracellular ORF7a binds to LPS. ORF7a has two ATP binding sites, "HYQEC" and "TYEGNS" . "HYQEC" is in the BPI1/LBP domain. B. Extracellular ORF7a binds to human CD14 antigen molecules.