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Like other tetraacyl partial structures of lipopolysaccharide
(LPS) and lipid A, LPS that has been partially deacylated by
acyloxyacyl hydrolase can inhibit LPS-induced responses in human cells.
To identify the site(s) of inhibition in the LPS recognition pathway,
we analyzed the apparent binding affinities and interactions of
Volume 270,
Number 17,
Issue of April 28, pp. 9904-9910, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
H-labeled enzymatically deacylated LPS (dLPS) and
[H]LPS with CD14, the LPS receptor, on THP-1
cells. Using (i) incubation conditions that prevented ligand
internalization and (ii) defined concentrations of LPS binding protein
(LBP), which facilitates LPS and dLPS binding to CD14, we found that
dLPS can antagonize LPS in at least three ways. 1) When the
concentration of LBP in the medium was suboptimal for promoting
LPS-CD14 binding, low concentrations of dLPS were able to compete with
LPS for binding CD14, suggesting competition between LPS and dLPS for
engaging LBP. 2) When LBP was present in excess, dLPS could compete
with LPS for binding CD14, but only at dLPS concentrations that were at
or above its Kfor binding CD14 (100
ng/ml). 3) In contrast, substoichiometric concentrations of dLPS (1
ng/ml) inhibited LPS-induced (3 ng/ml) interleukin-8 release without
blocking LPS binding to CD14. Functional antagonism was possible
without competition for cell-surface binding because both LPS-induced
interleukin-8 release and dLPS inhibition occurred at concentrations
that were far below their respective CD14 binding K
values. In addition to its expected ability to compete with LPS
for binding LBP and CD14, dLPS thus potently antagonizes LPS at an
undiscovered site that is distal to LPS-CD14 binding in the LPS
recognition pathway.
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