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Leukocyte activity is controlled by numerous interactions between membrane receptors and ligands on the cell surface. These interactions are of low affinity making detection difficult. We developed a sensitive assay that could readily detect extremely weak interactions such as that between CD200 and the activating receptor CD200RLa (K(d)>500 microM) at the protein level. We used the new technology to screen for interactions of inhibitory receptors for collagens. We confirmed that both human and mouse leukocyte-associated Ig-like receptor-1, and in addition the related inhibitory leukocyte Ig-like receptor subfamily B member 4 (CD85K, Gp49B), bound collagen specifically, whereas other cell surface proteins gave no binding. The monomeric affinities of the interactions were then determined to allow comparison with other leukocyte interactions and indicate conditions when these interactions might lead to inhibitory signals.

Original publication

DOI

10.1002/eji.200839188

Type

Journal article

Journal

Eur J Immunol

Publication Date

04/2009

Volume

39

Pages

1167 - 1175

Keywords

Amino Acid Sequence, Animals, Antigens, CD, Collagen, Humans, Immobilized Proteins, Leukocytes, Membrane Glycoproteins, Mice, Molecular Sequence Data, Receptors, Immunologic, Surface Plasmon Resonance