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Updated: Aug 11, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
Published on: June 13, 2014
Intercellular adhesion molecule-2 (CD102) binds to the leukocyte integrin CD11b/CD18 through the A domain
J Xie1, R Li, P Kotovuori
1Department of Biosciences, University of Helsinki, Finland.
Insights
Intercellular adhesion molecule-2 (ICAM-2) protein interacts with leukocyte function-associated antigen-1 (LFA-1) and Mac-1 (CD11/CD18). This study shows ICAM-2 binds to CD11b/CD18 via the CD11b A domain.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- Leukocyte adhesion is crucial for immune responses.
- Beta 2-integrins (CD11/CD18) mediate leukocyte adhesion by binding intercellular adhesion molecules (ICAMs).
- ICAM-1 binds CD11a/CD18 and CD11b/CD18; ICAM-2 binds CD11a/CD18.
Purpose of the Study:
- To investigate the interaction between ICAM-2 and CD11b/CD18.
- To identify the specific binding site of ICAM-2 on CD11b/CD18.
Main Methods:
- Protein-protein interaction assays.
- Analysis of binding domains using purified proteins and peptides.
Main Results:
- The ICAM-2 protein directly interacts with CD11b/CD18.
- Binding of ICAM-2 to CD11b/CD18 is mediated by the A domain of CD11b.
- A previously identified CD11a/CD18-binding peptide from ICAM-2 also binds CD11b/CD18.
Conclusions:
- ICAM-2 is a ligand for both CD11a/CD18 and CD11b/CD18.
- The CD11b A domain is critical for ICAM-2 binding.
- These findings expand the understanding of leukocyte adhesion molecule interactions.
Abstract:
The interactions between the leukocyte-specific beta 2-integrins cluster of differentiation (CD) Ag CD11/CD18 and their ligands, the intercellular adhesion molecules (ICAMs), play important roles in many adhesion-dependent leukocyte functions. ICAM-1 is known to be a ligand for both CD11a/CD18 and CD11b/CD18. ICAM-2, whose two extracellular Ig domains show the highest homology to the two NH2-terminal domains of ICAM-1, has been previously shown to be a ligand for CD11a/CD18. We recently found that a 22-amino acid CD11a/CD18-binding peptide, P1, derived from the first domain of ICAM-2, also binds to purified CD11b/CD18. In the present study, we demonstrate that the ICAM-2 protein interacts with CD11b/CD18, and the binding is through the CD11b A domain.
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