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Infection and Immunity, March 2000, p. 1259-1264, Vol. 68, No. 3
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Phospholipid Synthesis by Staphylococcus aureus during (Sub)Lethal Attack by Mammalian 14-Kilodalton Group IIA Phospholipase A2

Amy K. Foreman-Wykert,1,dagger Jerrold Weiss,2 and Peter Elsbach1,3,*

Department of Microbiology1 and Department of Medicine,3 New York University School of Medicine, New York, New York 10016, and Department of Internal Medicine and Microbiology, Division of Infectious Diseases, Inflammation Program, University of Iowa College of Medicine, Iowa City, Iowa 522422

Received 16 August 1999/Returned for modification 18 October 1999/Accepted 26 November 1999

Killing of gram-positive bacteria by mammalian group IIA phospholipases A2 (PLA2) requires the catalytic activity of the enzyme. However, nearly complete degradation of the phospholipids can occur with little effect on bacterial viability, suggesting that PLA2-treated bacteria can biosynthetically replace phospholipids that are lost due to PLA2 action. In the presence of albumin, phospholipid degradation products are quantitatively sequestered extracellularly. In the absence of albumin, the bacteria retain and substantially reutilize the phospholipid breakdown products and survive an otherwise lethal dose of PLA2. PLA2-treated bacteria also continue to incorporate sodium [2-14C]acetate into phospholipids, suggesting that the bacteria are attempting to repair the damaged membranes by de novo synthesis of phospholipids. To determine whether PLA2 action also triggers activation of bacterial lipolytic enzymes, the effects of nisin and PLA2 on the degradation of S. aureus lipids were compared. In contrast to nisin treatment, PLA2 treatment does not stimulate endogenous phospholipase activity in S. aureus. These findings show that S. aureus responds to PLA2 attack by continued phospholipid (re)synthesis by both de novo and salvage pathways. The fate of PLA2-treated S. aureus therefore appears to depend on the relative rates of phospholipid degradation and synthesis.

* Corresponding author. Mailing address: Department of Medicine, New York University School of Medicine, 550 First Ave., New York, NY 10016. Phone: (212) 263-5633. Fax: (212) 263-8276. E-mail: elsbap01{at}mcrcr.med.nyu.edu.

dagger Present address: Department of Microbiology, Immunology and Molecular Genetics, UCLA School of Medicine, Los Angeles, CA 90095.

Infection and Immunity, March 2000, p. 1259-1264, Vol. 68, No. 3
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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