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Effect of D-Alanylation of (Lipo)Teichoic Acids of Staphylococcus aureus on Host Secretory Phospholipase A₂ Action before and after Phagocytosis by Human Neutrophils¹

Catherine L. Hunt^*,, 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

Invading bacteria such as Staphylococcus aureus induce mobilization of professional phagocytes (e.g., neutrophils) and extracellular antibacterial proteins (e.g., group IIA phospholipase A₂ (gIIA PLA₂)). Accumulation of gIIA PLA₂ in inflammatory fluids confers potent extracellular antistaphylococcal activity and at lower concentrations promotes bacterial phospholipid degradation during phagocytosis of S. aureus by human neutrophils. D-alanylation of (lipo) teichoic acids of S. aureus increases bacterial resistance to gIIA PLA₂ 100-fold, raising the possibility that the resistance of ingested S. aureus to related gV and gX secretory PLA₂ present in human neutrophil granules depends on D-alanylation mediated by the dlt operon. However, we show that isogenic wild-type and dltA S. aureus are equally resistant to gV/X PLA₂ during phagocytosis and when exposed to the purified enzymes. The fates of wild-type and dltA S. aureus exposed to serum and human neutrophils differed significantly only when extracellular gIIA PLA₂ was also present before phagocytosis. The extreme potency of the gIIA PLA₂ toward dltA S. aureus suggests that even small amounts of this extracellular enzyme mobilized early in inflammation could contribute substantially to the overall cytotoxicity of acute inflammatory exudates toward S. aureus when D-alanylation of (lipo)teichoic acids is limiting.