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α‐Hemolysin, γ‐hemolysin, and leukocidin from Staphylococcus aureus : Distant in sequence but similar in structure
Author(s) -
Gouaux Eric,
Hobaugh Michael,
Song Langzhou
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560061216
Subject(s) - hemolysin , leukocidin , staphylococcus aureus , microbiology and biotechnology , panton–valentine leukocidin , biology , context (archaeology) , virulence , biochemistry , bacteria , genetics , methicillin resistant staphylococcus aureus , paleontology , gene
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.