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The membrane‐attack complex (MAC) of complement pathway and perforin (PF) are important tools deployed by the immune system to target pathogens. Both perforin and the C9 component of the MAC contain a common ‘MACPF’ domain and form pores in the cell membrane as part of their function. The MAC targets gram‐negative bacteria and certain pathogenic parasites, while perforin, released by natural killer cells or cytotoxic T lymphocytes (CTLs), targets virus‐infected and transformed host cells (1). Remarkably, recent structural studies show that the MACPF domain is homologous to the pore‐forming portion of bacterial cholesterol‐dependent cytolysins; these data have provided important insight into the mechanism of pore‐forming MACPF proteins. In addition to their role in immunity, MACPF family members have been identified as animal venoms, factors required for pathogen migration across host cell …