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*
Division of Experimental Immunology and Immunopathology, Department of Pathology, and
Department of Microbiology and Immunology, University of Louisville, Louisville, KY 40292
CR3 (Mac-1; 
Mß2 integrin) functions as
both a receptor for the opsonic iC3b fragment of C3 triggering
phagocytosis or cytotoxicity and an adhesion molecule mediating
leukocyte diapedesis. Recent reports have suggested that a CR3 lectin
site may be required for both cytotoxic responses and adhesion.
Cytotoxic responses require dual recognition of iC3b via the I domain
of CD11b and specific microbial surface polysaccharides (e.g.,
ß-glucan) via a separate lectin site. Likewise, adhesion requires a
lectin-dependent membrane complex between CR3 and CD87. To characterize
the lectin site further, a recombinant baculovirus (rBv) system was
developed that allowed high level expression of rCD11b on membranes and
in the cytoplasm of Sf21 insect cells. Six rBv were generated that
contained truncated cDNA encoding various CD11b domains. Immunoblotting
of rBv-infected Sf21 cells showed that some native epitopes were
expressed by five of six rCD11b fragments. Lectin activity of rCD11b
proteins was evaluated by both flow cytometry with ß-glucan-FITC and
radioactive binding assays with [125I]ß-glucan. Sf21
cells expressing rCD11b that included the C-terminal region, with or
without the I-domain, exhibited lectin activity that was inhibited by
unlabeled ß-glucan or anti-CR3 mAbs. The smallest rCD11b fragment
exhibiting lectin activity included the C-terminus and part of the
divalent cation binding region. The ß-glucan binding affinities of
the three C-terminal region-containing rCD11bs expressed on Sf21 cell
membranes were not significantly different from each other and were
similar to that of neutrophil CR3. These data suggest that the lectin
site may be located entirely within CD11b, although lectin
site-dependent signaling through CD18 probably occurs with the
heterodimer.
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