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Papers In Press, published online ahead of print November 2, 2001
Chemistry and Biochemistry, Univ. of Washington, Seattle, WA 98195
Corresponding Author: gelb{at}chem.washington.edu
Group IIA secreted phospholipase A2 (sPLA2) is known to display potent gram-positive bactericidal activity in vitro and in vivo. We have analysed 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 Escherichia 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 Staphylococcus 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 sPLA2’s putative membrane binding surface 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; 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.
J. Biol. Chem, 10.1074/jbc.M109699200
Submitted on October 8, 2001
Revised on November 2, 2001
Accepted on November 2, 2001
Bactericidal properties of human and murine groups I, II, V, X, and XII secreted phospholipases A2
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