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Journal of Lipid Research, Vol 38, 516-525, Copyright © 1997 by Lipid Research, Inc.
T Massamiri, PS Tobias and LK Curtiss
The interaction of lipopolysaccharide binding protein (LBP) with
apolipoprotein (apo)A-I on high density lipoproteins (HDL) was studied in
solid phase ligand binding assays with a biotinylated LBP-specific
antibody. The association was dependent on LBP concentration and enhanced
in the presence of lipopolysaccharide (LPS). Maximal enhancement was
measured at an LPS/LBP molar ratio of 6. To identify regions on apoA-I that
participate directly or indirectly in the interaction between LBP and HDL,
we attempted to inhibit LBP association with a panel of mapped
apoA-I-specific monoclonal antibodies. Whereas some antibodies were
effective inhibitors, others were not, even though they bound apoA-I.
Furthermore, selected apoA-I synthetic peptides inhibited the
antibody-mediated interference of the HDL/LBP interaction. Although no
specific mechanism can be defined for the basis of the inhibitory effects
of the antibodies on the association of LBP with HDL, we identified a role
for three unique regions on apoA-I between residues 1-31, 95-164, and
178-200. These results suggested that apoA-I is a key component in the
association of LBP with HDL and may play an important role in the biologic
activity of LPS/LBP complexes.
ARTICLES
Structural determinants for the interaction of lipopolysaccharide binding protein with purified high density lipoproteins: role of apolipoprotein A-I
Department of Immunology, Scripps Research Institute, La Jolla, CA 92037, USA.
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