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The Journal of Immunology, 2001, 166: 4029-4034.
Copyright © 2001 by The American Association of Immunologists

Bactericidal Properties of Group IIA and Group V Phospholipases A21

Juha O. Grönroos*, Veli J. O. Laine*, Marcel J. W. Janssen{dagger}, Maarten R. Egmond{dagger} and Timo J. Nevalainen2,*

* Department of Pathology, University of Turku and Turku University Hospital, Turku, Finland; and {dagger} Department of Enzymology and Protein Engineering, CBLE Institute of Biomembranes, University of Utrecht, Utrecht, The Netherlands

Group V phospholipase A2 (PLA2) is a recently characterized 14-kDa secretory PLA2 of mammalian heart and macrophage-derived cells. Group IIA PLA2, which is structurally close to group V PLA2, has been shown to kill Gram-positive bacteria in vitro and to prevent symptoms of Gram-positive infection in vivo. We studied the antibacterial properties of fully active recombinant rat group IIA and V PLA2s. Both group IIA and V PLA2s were highly bactericidal against Gram-positive bacteria, including methicillin-resistant staphylococci and vancomycin-resistant enterococci. Only high concentrations of group IIA PLA2 showed some bactericidal effect against the Gram-negative bacterium Escherichia coli. Our results confirm that group IIA PLA2 is a potent antibacterial enzyme against Gram-positive bacteria. Moreover, we show here that group V PLA2 is a novel antibacterial mammalian protein, but is less potent than group IIA PLA2. Both enzymes may be considered as future therapeutic agents against bacterial infections.




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