The staphylococcal toxin Panton-Valentine Leukocidin targets human C5a receptors

Cell Host Microbe. 2013 May 15;13(5):584-594. doi: 10.1016/j.chom.2013.04.006.


Panton-Valentine Leukocidin (PVL) is a staphylococcal bicomponent pore-forming toxin linked to severe invasive infections. Target-cell and species specificity of PVL are poorly understood, and the mechanism of action of this toxin in Staphylococcus aureus virulence is controversial. Here, we identify the human complement receptors C5aR and C5L2 as host targets of PVL, mediating both toxin binding and cytotoxicity. Expression and interspecies variations of the C5aR determine cell and species specificity of PVL. The C5aR binding PVL component, LukS-PV, is a potent inhibitor of C5a-induced immune cell activation. These findings provide insight into leukocidin function and staphylococcal virulence and offer directions for future investigations into individual susceptibility to severe staphylococcal disease.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / metabolism
  • Bacterial Toxins / metabolism*
  • Bacterial Toxins / toxicity
  • Cells, Cultured
  • Exotoxins / metabolism*
  • Exotoxins / toxicity
  • Host-Pathogen Interactions*
  • Humans
  • Leukocidins / metabolism*
  • Leukocidins / toxicity
  • Receptor, Anaphylatoxin C5a / metabolism*
  • Receptors, Chemokine / metabolism
  • Staphylococcus aureus / immunology*
  • Staphylococcus aureus / pathogenicity*


  • Bacterial Proteins
  • Bacterial Toxins
  • C5aR2 protein, human
  • Exotoxins
  • Leukocidins
  • Panton-Valentine leukocidin
  • Receptor, Anaphylatoxin C5a
  • Receptors, Chemokine
  • leukocidin S-component protein, Staphylococcus