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Research Article Free access | 10.1172/JCI118399

The potent anti-Staphylococcus aureus activity of a sterile rabbit inflammatory fluid is due to a 14-kD phospholipase A2.

Y Weinrauch, P Elsbach, L M Madsen, A Foreman, and J Weiss

Department of Microbiology, New York University School of Medicine, New York 10016, USA.

Find articles by Weinrauch, Y. in: JCI | PubMed | Google Scholar

Department of Microbiology, New York University School of Medicine, New York 10016, USA.

Find articles by Elsbach, P. in: JCI | PubMed | Google Scholar

Department of Microbiology, New York University School of Medicine, New York 10016, USA.

Find articles by Madsen, L. in: JCI | PubMed | Google Scholar

Department of Microbiology, New York University School of Medicine, New York 10016, USA.

Find articles by Foreman, A. in: JCI | PubMed | Google Scholar

Department of Microbiology, New York University School of Medicine, New York 10016, USA.

Find articles by Weiss, J. in: JCI | PubMed | Google Scholar

Published January 1, 1996 - More info

Published in Volume 97, Issue 1 on January 1, 1996
J Clin Invest. 1996;97(1):250–257. https://doi.org/10.1172/JCI118399.
© 1996 The American Society for Clinical Investigation
Published January 1, 1996 - Version history
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Abstract

The cell-free fluid (ascitic fluid, AF) of a sterile inflammatory peritoneal exudate elicited in rabbits is potently bactericidal for complement-resistant gram-negative as well as gram-positive bacterial species. This activity is absent in plasma. We now show that essentially all activity in AF against Staphylococcus aureus is attributable to a group II 14-kD phospholipase A2 (PLA2), previously purified from AF in this laboratory. Antistaphylococcal activity of purified PLA2 and of whole AF containing a corresponding amount of PLA2 was comparable and blocked by anti-AF-PLA2 serum. At concentrations present in AF (approximately 10 nM), AF PLA2 kills > 2 logs of 10(6) S. aureus/ml, including methicillin-resistant clinical isolates, and other species of gram-positive bacteria. Human group II PLA2 displays similar bactericidal activity toward S. aureus (LD90 approximately 1-5 nM), whereas 14-kD PLA2 from pig pancreas and snake venom are inactive even at micromolar doses. Bacterial killing by PLA2 requires Ca2+ and catalytic activity and is accompanied by bacterial phospholipolysis and disruption of the bacterial cell membrane and cell wall. These findings reveal that group II extracellular PLA2, the function of which at inflammatory sites has been unclear, is an extraordinarily potent endogenous antibiotic against S. aureus and other gram-positive bacteria.

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