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Leukocidin GH is a potent bicomponent pore-forming cytotoxin secreted by Staphylococcus aureus. It consists of two protein subunits, LukG and LukH, which form a stable heterodimer in solution before binding to the complement receptor 3 (CD11b) on the surface of human phagocytic cells such as neutrophils, monocytes, and macrophages. Upon binding, several dimers assemble into a membrane-inserting octameric pore, causing lysis of the host cell. This mechanism allows S. aureus to evade the immune system by directly killing host phagocytes. Unlike most other leukocidins, LukGH shows substantial sequence variability and species specificity, with limited activity toward murine cells. LukGH (also known as LukAB) is considered a central virulence factor implicated in S. aureus infections—including skin and soft tissue infections, sepsis, and pneumonia—and is a current target for antibody-mediated neutralization strategies in early-stage research.
Direct binding to the α-subunit of complement receptor 3 (CD11b) on human phagocytic cells, leading to oligomerization, pore formation, cell lysis, and immune evasion
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