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Leukocidin subunit G (LukG), also known as LukB, is the F-component of the bicomponent pore-forming toxin LukGH (or LukAB) secreted by Staphylococcus aureus (UniProt Q2FWP0) [1]. This toxin is a critical virulence factor that specifically targets and kills human phagocytes, such as neutrophils and macrophages, by forming octameric pores in their plasma membranes (Dumont et al., 2011) [2]. LukG pairs with its partner subunit, Leukocidin subunit H (LukH/LukA), to bind to the CD11b receptor on the surface of host cells (DuMont et al., 2013) [3]. By destroying these key immune cells, LukGH facilitates bacterial survival and dissemination during invasive infections, including pneumonia and bacteremia (Thammavongsa et al., 2015) [4]. Therapeutic strategies targeting LukG primarily involve neutralizing monoclonal antibodies, such as ASN-2, designed to block pore formation and restore the host's ability to clear the infection (Arsanis, 2018) [5]. Despite the failure of some clinical trials, LukG remains a significant target for anti-virulence therapies aimed at antibiotic-resistant S. aureus strains.
Neutralization of the toxin subunit to prevent assembly of the octameric pore on the host cell membrane and block binding to the CD11b receptor.
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