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Department of Immunology, Duke University Medical Center, Durham, NC 27710
The ability of chemokines to bind to glycosaminoglycans (GAGs) on
cell surfaces and in the extracellular matrix is thought to play a
crucial role in chemokine function. We investigated the structural
basis for chemokine binding to GAGs by using in vitro mutagenesis to
identify amino acids of chemokine macrophage-inflammatory protein-1ß
(MIP-1ß) that contribute to its interaction with the model GAG
heparin. Among six basic residues that are organized into a single
basic domain in the folded MIP-1ß monomer, three (R18, K45, and R46)
were found to contribute significantly to heparin binding. Of these,
R46 was found to play a dominant role, and proved essential for the
interaction of MIP-1ß with both heparin and heparan sulfate in
physiological salt. The results of this mutational analysis have
implications for the structure of the MIP-1ß-heparin complex, and a
comparison of these results with those obtained by mutational analysis
of the MIP-1
-heparin interaction suggests a possible structural
difference between the MIP-1ß-heparin and MIP-1-heparin complexes.
To determine whether GAG binding plays an important role in receptor
binding and cellular activation by MIP-1ß, the activities of
wild-type MIP-1ß and R46-substituted MIP-1ß were compared in assays
of T lymphocyte chemotaxis. The two proteins proved equipotent in this
assay, arguing that interaction of MIP-1ß with GAGs is not
intrinsically required for functional interaction of MIP-1ß with its
receptor.
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