Binding of the integrin Mac-1 (CD11b/CD18) to the third immunoglobulin-like domain of ICAM-1 (CD54) and its regulation by glycosylation

Cell. 1991 Jun 14;65(6):961-71. doi: 10.1016/0092-8674(91)90548-d.


Both the integrins LFA-1 and Mac-1 bind to ICAM-1, an immunoglobulin superfamily member. Previously, we localized the binding sites of LFA-1 and the major group of human rhinoviruses to the first NH2-terminal immunoglobulin-like domain of ICAM-1. Here, we show that the binding site on ICAM-1 for Mac-1 is unexpectedly distinct from that for LFA-1 and maps to the third NH2-terminal immunoglobulin-like domain. These findings provide a function for the tandem duplication of immunoglobulin-like domains in ICAM-1 and have implications for other immunoglobulin superfamily members. Mutations at two sites in the third domain that destroy consensus sequences for N-linked glycosylation enhance binding to purified Mac-1. Agents that interfere with carbohydrate processing provide evidence that the size of the N-linked oligosaccharide side chains on ICAM-1 affects binding to Mac-1 but not to LFA-1. Thus, we suggest that the extent of glycosylation on ICAM-1 may regulate adhesion to LFA-1 or Mac-1 in vivo.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cell Adhesion
  • Cell Adhesion Molecules / metabolism*
  • DNA Mutational Analysis
  • Glycoproteins / metabolism
  • Glycosylation
  • Humans
  • In Vitro Techniques
  • Intercellular Adhesion Molecule-1
  • Lymphocyte Function-Associated Antigen-1 / metabolism
  • Macrophage-1 Antigen / metabolism*
  • Neutrophils / cytology
  • Protein Binding
  • Recombinant Proteins / metabolism
  • Structure-Activity Relationship


  • Cell Adhesion Molecules
  • Glycoproteins
  • Lymphocyte Function-Associated Antigen-1
  • Macrophage-1 Antigen
  • Recombinant Proteins
  • Intercellular Adhesion Molecule-1