A membrane attack complex domain is present in the Plasmodium sporozoite protein . Before hepatocyte infection, it destroys the sinusoidal cell layer. The molecule's pore-forming activity is required for sporozoites to pass through the host's plasma membrane . Similar to the complement membrane attack complex, the SARS-CoV-2 protein can also construct cell membrane pores. Near the transmembrane region of the SARS-CoV-2 S protein, the HAP2/GCS1 and Izumo-Ig domains promote the formation of membrane fusion pores . This overlapping region contains Ca2+-ATPase, actin-myosin motor, and phospholipid flippase structures. These sequences are involved in Ca2+-dependent hemolysis and coagulation. The membrane attack complex (MAC, C5b-9) can perforate the membrane of a target cell . S also contains a membrane attack complex domain, which can be involved in forming fusion pores invading red blood cells. Hemolysin is a type of perforin that specifically targets infected cells. Hemolysin is more resistant to heat . The fusion protein of the small ruminant plague virus is a hemolysin . Newcastle disease virus hemolysin( ) is sufficient to lyse red blood cells . Measles virus hemolysin shares many properties with myxovirus hemolysin . It predisposes red blood cells to hemagglutination and hemolysis. Equine encephalomyelitis viruses are hemolytic over a wide temperature range . Specific pH changes reduced their hemolytic activity. However, trypsin treatment significantly increased the viruses' hemagglutinating activity . Under conditions of heating, formaldehyde, and ultraviolet radiation, the mumps virus retains almost all of its hemolytic activity and infectivity . SARS-CoV-2 nsp3 is a component of the organelle's double-membrane pore complex . On the proteoliposome bilayer membrane, the SARS-CoV-2 ORF3a polymer forms a Ca 2+ channel . SARS-CoV-2 ORF8 is a very short membrane peptide with a single channel span. It forms cation-selective channels when assembled in lipid bilayers . ORF3a and ORF8 have pore-forming properties. It suggested that they were SARS-CoV-2 hemolysin proteins. ORF3a is capable of forming not only dimers but also tetramers . Then it can form larger hemolytic pores in the cell membrane. It may be a critical entry point for viral proteins into the host cell.