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¹ Department of Immunology, ² Thrombosis & Haemostasis Laboratory, and ³ Department of Physiological Chemistry, University Medical Center, 3584 EA Utrecht, Netherlands
⁴ Center for Biochemistry, Center for Molecular Medicine, and Department of Dermatology, University of Cologne, D50931 Köln, Germany
⁵ Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK
⁶ Division of Cell Biology, Netherlands Cancer Institute, 1066 CX Amsterdam, Netherlands

CORRESPONDENCE Linde Meyaard: l.meyaard{at}umcutrecht.nl

Collagens are the most abundant proteins in the human body, important in maintenance of tissue structure and hemostasis. Here we report that collagens are high affinity ligands for the broadly expressed inhibitory leukocyte-associated immunoglobulin-like receptor-1 (LAIR-1). The interaction is dependent on the conserved Gly-Pro-Hyp collagen repeats. Antibody cross-linking of LAIR-1 is known to inhibit immune cell function in vitro. We now show that collagens are functional ligands for LAIR-1 and directly inhibit immune cell activation in vitro. Thus far, all documented ligands for immune inhibitory receptors are membrane molecules, implying a regulatory role in cell–cell interaction. Our data reveal a novel mechanism of peripheral immune regulation by inhibitory immune receptors binding to extracellular matrix collagens.

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