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. 2009 Mar 20;284(12):7495–7504. doi: 10.1074/jbc.M808643200

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Copyright © 2009, The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 7. — SP-A interacted with the I-domain of CR3. Binding of SP-A to CR3 was determined as outlined in the legend to Fig. 5. β-Glucan (binds the lectin domain of CR3) reduced the binding to SP-A (panel A). Antibodies to the I-domain of CR3 (M1/70 and CBRM1/5) almost completely blocked binding of SP-A to CR3 (panel A). Collagenase treatment of SP-A (colSPA) reduced the binding to CR3 compared with native SP-A. A further reduction in binding of collagenase-treated SP-A to CR3 was observed in the presence of β-glucan and M1/70 antibody (panel B) suggesting a role for the both the I-domain and lectin domain in CR3/SP-A interactions. Deglycosylation of SPA (degSPA) also reduced binding to CR3 compared with native SP-A and this binding was not inhibited in the presence of β-glucan. In contrast, the addition of the M1/70 antibody to the I-domain reduced binding of deglycosylated SP-A to CR3 (panel C), which implicates the collagen domain in the interaction with the I-domain. Data are mean ± S.E. with n = 4 experiments per group, *, p < 0.05 compared with binding of iC3b; #, p < 0.05 compared with human SP-A (panel A). *, p < 0.05 compared with human SPA; #, p < 0.05 compared with collagenase SPA or deglycosylated SPA (panels B and C).