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J. Biol. Chem., Vol. 277, Issue 49, 47636-47644, December 6, 2002
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From the Departments of Mammalian Group IIA phospholipases
A2 (PLA2) potently kill
Staphylococcus aureus. Highly cationic properties of these
PLA2 are important for Ca2+-independent
binding and cell wall penetration, prerequisites for
Ca2+-dependent degradation of membrane
phospholipids and bacterial killing. To further delineate charge
properties of the bacterial envelope important in Group IIA
PLA2 action against S. aureus, we examined the
effects of mutations that prevent specific modifications of cell wall
(dltA) and cell membrane (mprF) polyanions. In
comparison to the parent strain, isogenic
dltA
Role of Charge Properties of Bacterial Envelope in
Bactericidal Action of Human Group IIA Phospholipase A2
against Staphylococcus aureus*
§,
,§§§
Microbiology,
Internal Medicine, and the
§ Inflammation Program, University of Iowa, Iowa City
Veterans Affairs Medical Center, Iowa City, Iowa 52246, the
¶ Mikrobielle Genetik, Universität Tübingen, Auf der
Morgenstelle 28, 72076 Tübingen, Germany, the Departments
of Chemistry and Biochemistry, University of Washington, Seattle,
Washington 98195-1700, and the ** Department of Pharmacy,
Guangxi Cancer Hospital/Institute, Nanning City, Guangxi Province
530021, Peoples Republic of China
bacteria are ~30-100× more sensitive
to PLA2, whereas mprF bacteria
are <3-fold more sensitive. Differences in PLA2
sensitivity of intact bacteria reflect differences in cell wall, not
cell membrane, properties since protoplasts from all three strains are
equally sensitive to PLA2. A diminished positive charge in PLA2 reduces PLA2 binding and antibacterial
activity. In contrast, diminished cell wall negative charge by
substitution of (lipo)teichoic acids with D-alanine reduces
antibacterial activity of bound PLA2, but not initial
PLA2 binding. Therefore, the potent
antistaphylococcal activity of Group IIA PLA2 depends on
cationic properties of the enzyme that promote binding to the cell
wall, and polyanionic properties of cell wall (lipo)teichoic acids that
promote attack of membrane phospholipids by bound PLA2.
*
This work was supported by United States Public Health
Service Grant AI-18571 (to J. W.) and National Institutes of Health Grant HL36235 (to M. H. G.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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