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J. Biol. Chem., Vol. 269, Issue 42, 26331-26337, Oct, 1994
J Weiss, M Inada, P Elsbach and RM Crowl
Extracellular 14-kDa phospholipases A2 (PLA2) in inflammatory exudates can
contribute to bacterial phospholipid (PL) degradation during phagocytosis
of Escherichia coli by polymorphonuclear leukocytes (PMN) and are highly
active toward E. coli treated with the bactericidal/permeability-increasing
protein (BPI) purified from PMN. PLA2 activity toward BPI-treated E. coli
varies greatly among members of this conserved family of enzymes and
apparently depends on a cluster of basic residues in a variable surface
region near the NH2 terminus for recognition of this biological target
(Weiss, J., Wright, G.W., Bekkers, A.C.A.P.A., van den Bergh, C.J., and
Verheij, H.M. (1991) J. Biol. Chem. 266, 4162-4167). We have examined by
site-specific mutagenesis of a recombinant PLA2 that is identical to an
enzyme in human synovial fluid (containing His-6, Arg-7, Lys-10, and Lys-15
and a global net charge of +15) the role of basic residues in this region
in PLA2 action against PLA-deficient (pldA-) E. coli. Substitution of Ser
for Arg-7 +/- Gln for Lys-15 caused, respectively, about a 10- and 25- fold
reduction in BPI-dependent PLA2 binding and activity to E. coli, but had no
effect on hydrolysis of PL of autoclaved E. coli or dispersions of purified
PL. PL degradation during phagocytosis was increased after pretreatment of
E. coli (or PMN) with wild-type PLA2 followed by removal of unbound PLA2.
Thus, the PLA2 binds to cells before phagocytosis followed by
internalization of the enzyme along with E. coli and intracellular action.
Mutant (e.g. R7S +/- K15Q) PLA2 show the same BPI-independent binding to E.
coli as the wild-type enzyme but 10-30-fold reduced activity during
phagocytosis, reflecting lower intracellular activity of these enzymes.
Thus, structural determinants first implicated in PLA2 action toward E.
coli treated with purified BPI apparently are also important in the
intracellular action of PLA2 during phagocytosis by PMN.
Structural determinants of the action against Escherichia coli of a human inflammatory fluid phospholipase A2 in concert with polymorphonuclear leukocytes
Department of Microbiology, New York University School of Medicine, New York 10016.
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