Panton-Valentine leukocidin subunit S (LukS-PV)

Panton-Valentine leukocidin subunit S (LukS-PV) is one component of the bicomponent Panton-Valentine leukocidin (PVL) toxin produced by Staphylococcus aureus. It works in conjunction with the F subunit (LukF-PV) to form pores in the membranes of host cells, particularly leukocytes. The protein has a structure consisting of three functional subdomains: a central β-sandwich, a protruding rim, and a stem domain that is critical for pore formation[1][3]. LukS-PV specifically binds to the human C5a receptor (hC5aR1) on target cells, while LukF-PV interacts with CD45, and together they form an octameric pore structure with alternating S and F components[4]. This pore formation leads to cell lysis and contributes to the pathogenicity of PVL-producing S. aureus strains. The signal peptide of LukS-PV has been shown to mediate increased adhesion to heparan sulfates[5]. LukS-PV has been directly implicated in the pathophysiology of necrotizing pneumonia, where it can be detected in lung sections of affected patients. It induces apoptosis by targeting mitochondria, causing the release of cytochrome c and other pro-apoptotic factors, leading to caspase activation and DNA fragmentation[2]. This process occurs independently of Bax, a pro-apoptotic protein typically involved in mitochondrial pore formation.

Other names

PVL S-componentLukS-PV

Forms heterooligomeric pores with LukF-PV in target cell membranes Binds to C5a receptor (hC5aR1) on target cells Interacts with heparan sulfates via signal peptide Targets mitochondria to induce apoptosis