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Synergy between Extracellular Group IIA Phospholipase A₂ and Phagocyte NADPH Oxidase in Digestion of Phospholipids of Staphylococcus aureus Ingested by Human Neutrophils¹

Jon K. Femling^*,, William M. Nauseef^*,, and Jerrold P. Weiss^2,*,,

^* The Inflammation Program, Department of Microbiology, and Department of Medicine, University of Iowa and Veterans Affairs Medical Center, Iowa City, IA 52242

Acute inflammatory responses to invading bacteria such as Staphylococcus aureus include mobilization of polymorphonuclear leukocytes (PMN) and extracellular group IIA phospholipase A₂ (gIIA-PLA₂). Although accumulating coincidentally, the in vitro anti-staphylococcal activities of PMN and gIIA-PLA₂ have thus far been studied separately. We now show that degradation of S. aureus phospholipids during and after phagocytosis by human PMN requires the presence of extracellular gIIA-PLA₂. The concentration of extracellular gIIA-PLA₂ required to produce bacterial digestion was reduced 10-fold by PMN. The effects of added gIIA-PLA₂ were greater when present before phagocytosis but even apparent when added after S. aureus were ingested by PMN. Related group V and X PLA₂, which are present within PMN granules, do not contribute to bacterial phospholipid degradation during and after phagocytosis even when added at concentrations 30-fold higher than that needed for action of the gIIA-PLA₂. The action of added gIIA-PLA₂ required catalytically active gIIA-PLA₂ and, in PMN, a functional NADPH oxidase but not myeloperoxidase. These findings reveal a novel collaboration between cellular oxygen-dependent and extracellular oxygen-independent host defense systems that may be important in the ultimate resolution of S. aureus infections.

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