The I domain is a major recognition site on the leukocyte integrin Mac- 1 (CD11b/CD18) for four distinct adhesion ligands

doi:10.1083/jcb.120.4.1031

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The I domain is a major recognition site on the leukocyte integrin Mac- 1 (CD11b/CD18) for four distinct adhesion ligands

MS Diamond, J Garcia-Aguilar, JK Bickford, AL Corbi and TA Springer
Committee on Cell and Developmental Biology, Harvard Medical School, Boston, Massachusetts.

Despite the identification and characterization of several distinct ligands for the leukocyte integrin (CD11/CD18) family of adhesion receptors, little is known about the structural regions on these molecules that mediate ligand recognition. In this report, we use alpha subunit chimeras of Mac-1 (CD11b/CD18) and p150,95 (CD11c/CD18), and an extended panel of newly generated and previously characterized mAbs specific to the alpha chain of Mac-1 to map the binding sites for four distinct ligands for Mac-1: iC3b, fibrinogen, ICAM-1, and the as-yet uncharacterized counter-receptor responsible for neutrophil homotypic adhesion. Epitopes of mAbs that blocked ligand binding were mapped with the chimeras and used to localize the ligand recognition sites because the data obtained from functional assays with the Mac-1/p150,95 chimeras were not easily interpreted. Results show that the I domain on the alpha chain of Mac-1 is an important recognition site for all four ligands, and that the NH2-terminal and perhaps divalent cation binding regions but not the COOH-terminal segment may contribute. The recognition sites in the I domain appear overlapping but not identical as individual Mac-1-ligand interactions are distinguished by the discrete patterns of inhibitory mAbs. Additionally, we find that the alpha subunit NH2-terminal region and divalent cation binding region, despite being separated by over 200 amino acids of the I domain, appear structurally apposed because three mAbs require the presence of both of these regions for antigenic reactivity, and chimeras that contain the NH2 terminus of p150,95 require the divalent cation binding region of p150,95 to associate firmly with the beta subunit.
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Balsam, L. B., Liang, T. W., Parkos, C. A. (1998). Functional Mapping of CD11b/CD18 Epitopes Important in Neutrophil-Epithelial Interactions: A Central Role of the I Domain. J. Immunol. 160: 5058-5065 [Abstract] [Full Text]
Petruzzelli, L., Maduzia, L., Springer, T. A. (1998). Differential Requirements for LFA-1 Binding to ICAM-1 and LFA-1-Mediated Cell Aggregation. J. Immunol. 160: 4208-4216 [Abstract] [Full Text]
Oxvig, C., Springer, T. A. (1998). Experimental support for a beta -propeller domain in integrin alpha -subunits and a calcium binding site on its lower surface. Proc. Natl. Acad. Sci. USA 95: 4870-4875 [Abstract] [Full Text]
Bella, J., Kolatkar, P. R., Marlor, C. W., Greve, J. M., Rossmann, M. G. (1998). The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand. Proc. Natl. Acad. Sci. USA 95: 4140-4145 [Abstract] [Full Text]
Feng, Y., Chung, D., Garrard, L., McEnroe, G., Lim, D., Scardina, J., McFadden, K., Guzzetta, A., Lam, A., Abraham, J., Liu, D., Endemann, G. (1998). Peptides Derived from the Complementarity-determining Regions of Anti-Mac-1 Antibodies Block Intercellular Adhesion Molecule-1 Interaction with Mac-1. J. Biol. Chem. 273: 5625-5630 [Abstract] [Full Text]
Mesri, M., Plescia, J., Altieri, D. C. (1998). Dual Regulation of Ligand Binding by CD11b I Domain. INHIBITION OF INTERCELLULAR ADHESION AND MONOCYTE PROCOAGULANT ACTIVITY BY A FACTOR X-DERIVED PEPTIDE. J. Biol. Chem. 273: 744-748 [Abstract] [Full Text]
Pujades, C., Alon, R., Yauch, R. L., Masumoto, A., Burkly, L. C., Chen, C., Springer, T. A., Lobb, R. R., Hemler, M. E. (1997). Defining Extracellular Integrin alpha -Chain Sites That Affect Cell Adhesion and Adhesion Strengthening without Altering Soluble Ligand Binding. Mol. Biol. Cell 8: 2647-2657 [Abstract] [Full Text]
Parkos, C. A. (1997). I. Neutrophil adhesive interactions with intestinal epithelium. Am. J. Physiol. Gastrointest. Liver Physiol. 273: G763-G768 [Abstract] [Full Text]
Ho, W.-c., Heinemann, C., Hangan, D., Uniyal, S., Morris, V. L., Chan, B. M.C. (1997). Modulation of In Vivo Migratory Function of alpha 2beta 1 Integrin in Mouse Liver. Mol. Biol. Cell 8: 1863-1875 [Abstract] [Full Text]
Knorr, R., Dustin, M. L. (1997). The Lymphocyte Function-associated Antigen 1 I Domain Is a Transient Binding Module for Intercellular Adhesion Molecule (ICAM)-1 and ICAM-3 in Hydrodynamic Flow. JEM 186: 719-730 [Abstract] [Full Text]
Zhang, L., Plow, E. F. (1997). Identification and Reconstruction of the Binding Site within alpha Mbeta 2 for a Specific and High Affinity Ligand, NIF. J. Biol. Chem. 272: 17558-17564 [Abstract] [Full Text]
Marth, T., Kelsall, B. L. (1997). Regulation of Interleukin-12 by Complement Receptor 3 Signaling. JEM 185: 1987-1995 [Abstract] [Full Text]
Coulson, B. S., Londrigan, S. L., Lee, D. J. (1997). Rotavirus contains integrin ligand sequences and a disintegrin-like domain that are implicated in virus entry�into�cells. Proc. Natl. Acad. Sci. USA 94: 5389-5394 [Abstract] [Full Text]
Calderwood, D. A., Tuckwell, D. S., Eble, J., Kuhn, K., Humphries, M. J. (1997). The Integrin alpha 1 A-domain Is a Ligand Binding Site for Collagens and Laminin. J. Biol. Chem. 272: 12311-12317 [Abstract] [Full Text]
Huang, C., Springer, T. A. (1997). Folding of the beta -propeller domain of the integrin alpha L subunit is independent of the I domain and dependent on the beta 2�subunit. Proc. Natl. Acad. Sci. USA 94: 3162-3167 [Abstract] [Full Text]