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J Biol Chem, Vol. 273, Issue 15, 8680-8690, April 10, 1998
,
From the The hypothesis that soluble peptidoglycan (sPGN,
a macrophage-activator from Gram-positive bacteria) binds to CD14 (a
lipopolysaccharide (LPS) receptor) was tested. sPGN specifically bound
to CD14 in the following three assays: binding of soluble
32P-CD14 (sCD14) to agarose-immobilized sPGN,
enzyme-linked immunosorbent assay, and photoaffinity cross-linking.
sCD14 also specifically bound to agarose-immobilized muramyl dipeptide
or GlcNAc-muramyl dipeptide but not to PGN pentapeptide. Binding of
sCD14 to both sPGN and ReLPS (where ReLPS is LPS from Salmonella
minnesota Re 595) was competitively inhibited by unlabeled sCD14,
1-152 N-terminal fragment of sCD14, sPGN, smooth LPS, ReLPS, lipid A,
and lipoteichoic acid but not by dextran, dextran sulfate, heparin,
ribitol teichoic acid, or soluble low molecular weight PGN fragments.
Binding of sCD14 to sPGN was slower than to ReLPS but of higher
affinity (KD = 25 nM versus
41 nM). LPS-binding protein (LBP) increased the binding of
sCD14 to sPGN by adding another lower affinity KD
and another higher Bmax, but for ReLPS, LBP increased the affinity of binding by yielding two
KD with significantly higher affinity (7.1 and
27 nM). LBP also enhanced inhibition of sCD14
binding by LPS, ReLPS, and lipid A. Binding of sCD14 to both sPGN and
ReLPS was inhibited by anti-CD14 MEM-18 mAb, but other anti-CD14 mAbs
showed differential inhibition, suggesting conformational binding sites
on CD14 for sPGN and LPS, that are partially identical and partially
different.
Northwest Center for Medical Education,
Indiana University School of Medicine, Gary, Indiana 46408 and
the ¶ Department of Immunology, The Scripps Research Institute,
La Jolla, California 92037
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