Alpha-toxin binds to the membrane of eukaryotic cells (particularly red blood cells, RBC) forming pores, resulting in hemolysis, with the release of low-molecular weight molecules leading to eventual osmotic RBC lysis (PubMed:1587866, PubMed:20624979). Human RBCs bind much less alpha-toxin than do rabbit RBCs (PubMed:1587866, PubMed:20624979). Heptamer oligomerization and pore formation is required for lytic activity (PubMed:1587866, PubMed:20624979). Self-assembles to first form a non-lytic oligomeric intermediate, and then, a mushroom-shaped homoheptamer structure of 100 Angstroms in length and up to 100 Angstroms in diameter (PubMed:8943190) (Probable). Interacts with human ADAM10; this interaction is required for toxin pore formation, disruption of focal adhesions, and hly-mediated cytotoxicity (PubMed:20624979). Secreted as a monomer (PubMed:8943190). After oligomerization and pore formation, the complex is translocated across the bilayer, probably via the Gly-rich domain of each strand. The mushroom-shaped heptamer is composed of a cap domain (comprising 7 beta sandwiches and the amino latches of each protomer), 7 rim regions whose protruding strands may interact with the membrane bilayer, and the stem domain (52 Angstroms in length, 26 Angstroms in diameter) which forms the transmembrane pore. Belongs to the aerolysin family.