Panton-Valentine leukocidin F subunit (LukF-PV)

Panton-Valentine leukocidin (PVL) is a potent bi-component pore-forming toxin secreted by certain strains of Staphylococcus aureus, most notably community-acquired methicillin-resistant S. aureus (CA-MRSA) [PubMed: 15749820]. The toxin is composed of two distinct protein subunits, LukS-PV and LukF-PV, which act synergistically to destroy host immune cells [UniProt: P0A010]. LukF-PV serves as the second component in the assembly process; after LukS-PV binds to the C5a receptor on leukocytes, LukF-PV joins to form a hetero-octameric beta-barrel pore [PubMed: 24127485]. This pore disrupts the membrane integrity of neutrophils, monocytes, and macrophages, leading to cell death and the release of pro-inflammatory mediators [PubMed: 12689937]. Clinically, PVL is a major virulence factor associated with severe, necrotic skin infections and life-threatening necrotizing pneumonia [StatPearls: Panton-Valentine Leukocidin]. Therapeutic interventions include the use of antitoxin antibodies, such as those found in intravenous immunoglobulin (IVIG) or experimental monoclonal antibodies like ASN100, to neutralize the protein [ClinicalTrials.gov: NCT02940483]. Additionally, protein-synthesis-inhibiting antibiotics like clindamycin and linezolid are utilized to suppress the production of LukF-PV and its partner subunit at the genetic level [PubMed: 17307768].

Other names

LukF-PVPanton-Valentine leukocidin subunit FPVL-FLeukocidin F subunitPanton-Valentine leukocidin component F

Neutralization of the toxin subunits to prevent hetero-oligomerization and subsequent pore formation in host cell membranes [PubMed: 24127485].