Staphylococcus aureus Panton–Valentine leukocidin (PVL) (PVL)

Staphylococcus aureus Panton–Valentine leukocidin (PVL) is a bicomponent pore-forming cytotoxin that serves as a major virulence factor in specific strains of S. aureus, particularly community-acquired methicillin-resistant S. aureus (CA-MRSA) (Lina et al., 1999; PMID: 10548121). The toxin is composed of two distinct proteins, LukS-PV and LukF-PV, which are secreted independently and assemble into a heterooligomeric pore on the surface of host leukocytes (Spaan et al., 2013; PMID: 23761634). PVL specifically targets the C5a receptors (C5aR1 and C5aR2) on neutrophils, monocytes, and macrophages, leading to cell activation at low concentrations and necrotic cell death at higher concentrations (Spaan et al., 2013; PMID: 23761634). This leukocytolysis results in the release of reactive oxygen species and granular enzymes, contributing to severe tissue damage and necrotizing infections such as pneumonia and skin abscesses (Boyle-Vavra & Daum, 2007; PMID: 17341681). Clinical management often involves the use of protein synthesis inhibitors like linezolid or clindamycin, which effectively reduce the production of the toxin even at sub-inhibitory concentrations (Diep et al., 2007; PMID: 17908214). Additionally, intravenous immunoglobulin (IVIG) may be used to provide passive immunity by neutralizing the toxin subunits (Dumitrescu et al., 2007; PMID: 17654311).

Other names

PVLLukS-PV/LukF-PVPanton-Valentine toxinStaphylococcal Panton-Valentine leukocidin

Inhibition of toxin production through protein synthesis interference and neutralization of toxin subunits by antibodies.