α‐Hemolysin, γ‐hemolysin, and leukocidin from Staphylococcus aureus: Distant in sequence but similar in structure

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Abstract
α‐Hemolysin from Staphylococcus aureus assembles from a water‐soluble, monomeric species to a membrane‐bound heptamer on the surface of target cells, creating water‐filled channels that lead to cell death and lysis. Staphylococcus aureus also produces the γ‐hemolysin and leukocidin toxins, which function as two component toxins in the disruption and lysis of erythrocytes and leukocytes. Analysis of the aligned sequences of α‐hemolysin, γ‐hemolysin, and leukocidin in the context of the α‐hemolysin heptamer structure supports the conclusion that even though the level of sequence identity between α‐hemolysin and the γ‐hemolysin and leukocidin toxins is in the so‐called twilight zone, the three‐dimensional structures of the protomers are probably conserved. By analogy with α‐hemolysin, γ‐hemolysin and leukocidin may also form oligomeric, transmembrane channels in which an anti‐parallel β‐barrel constitutes the primary membrane‐embedded domain.

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