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

The staphylococcal toxin Panton-Valentine Leukocidin targets human C5a receptors.

Author information

1
Medical Microbiology, University Medical Center Utrecht, 3584CX Utrecht, The Netherlands.
2
CIRI, International Center for Infectiology Research, LabEx Ecofect, Université Lyon 1, 69007 Lyon, France; Inserm, U1111, 69007 Lyon, France; Ecole Normale Supérieure de Lyon, 69007 Lyon, France; CNRS, UMR5308, 69007 Lyon, France.
3
Medicinal Chemistry and Chemical Biology, Utrecht University, 3584CX Utrecht, The Netherlands.
4
CIRI, International Center for Infectiology Research, LabEx Ecofect, Université Lyon 1, 69007 Lyon, France; Inserm, U1111, 69007 Lyon, France; Ecole Normale Supérieure de Lyon, 69007 Lyon, France; CNRS, UMR5308, 69007 Lyon, France; Hospices Civils de Lyon, 69007 Lyon, France.
5
Medical Microbiology, University Medical Center Utrecht, 3584CX Utrecht, The Netherlands. Electronic address: j.vanstrijp@umcutrecht.nl.

Abstract

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.

PMID:
23684309
DOI:
10.1016/j.chom.2013.04.006
[Indexed for MEDLINE]
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