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J. Biol. Chem., Vol. 277, Issue 8, 5849-5857, February 22, 2002
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From the Group IIA secreted phospholipase
A2 (sPLA2) is known to display potent Gram-positive
bactericidal activity in vitro and in vivo. We
have analyzed the bactericidal activity of the full set of recombinant
murine and human groups I, II, V, X, and XII sPLA2s on Listeria
monocytogenes, Staphylococcus aureus, and
Escherichia coli. The rank order potency among human sPLA2s
against Gram-positive bacteria is group IIA > X > V > XII > IIE > IB, IIF (for murine sPLA2s: IIA > IID > V > IIE > IIC, X > IB, IIF), and only
human group XII displays detectable bactericidal activity against the Gram-negative bacterium E. coli. These studies show that
highly basic sPLA2s display potent bactericidal activity with the
exception of the ability of the acidic human group X sPLA2 to kill
Gram-positive bacteria. By studying the Bacillus subtilis
and S. aureus bactericidal potencies of a large panel of
human group IIA mutants in which basic residues were mutated to acidic
residues, it was found that: 1) the overall positive charge of the
sPLA2 is the dominant factor in dictating bactericidal potency; 2)
basic residues on the putative membrane binding surface of the sPLA2
are modestly more important for bactericidal activity than are other
basic residues; 3) relative bactericidal potency tracks well with the
ability of these mutants to degrade phospholipids in the bacterial
membrane; and 4) exposure of the bacterial membrane of Gram-positive
bacteria by disruption of the cell wall dramatically reduces the
negative effect of charge reversal mutagenesis on bactericidal potency.
Bactericidal Properties of Human and Murine Groups I, II, V, X,
and XII Secreted Phospholipases A2*
,
, and**
Departments of Chemistry and Biochemistry,
University of Washington, Seattle, Washington 98195, § Department of Pathology, University of Turku and Turku
University Hospital, 20520 Turku, Finland, and ¶ Institut
de Pharmacologie Moléculaire et Cellulaire, CNRS-UPR 411, 660 Route des Lucioles, Sophia Antipolis 06560 Valbonne, France
*
This work was supported by Grant HL36236 from the National
Institutes of Health (to M. H. G.), the research fund of the Turku University Hospital (to T. N.), and the CNRS, the Association pour la
Recherche sur le Cancer, and the Fonds de Recherche Hoechst Marion
Roussel (to G. L.).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.
To whom correspondence may be addressed. Tel.: 358-2-3337217;
E-mail: timo.nevalainen@utu.fi.
**
To whom correspondence may be addressed. Tel.: 206-543-7142; Fax:
206-685-8665; E-mail: gelb@chem.washington.edu.
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