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Brief Definitive Report

Department of Pathology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814

Address correspondence to Dr. Gabriela S. Dveksler, Department of Pathology, USUHS, 4301 Jones Bridge Rd., Bethesda, MD 20814-4799. Phone: 301-295-3332; Fax: 301-295-1640; E-mail: gdveksler{at}usuhs.mil

Pregnancy-specific glycoproteins (PSGs) are a family of highly similar secreted proteins produced by the placenta. PSG homologs have been identified in primates and rodents. Members of the human and murine PSG family induce secretion of antiinflammatory cytokines in mononuclear phagocytes. For the purpose of cloning the receptor, we screened a RAW 264.7 cell cDNA expression library. The PSG17 receptor was identified as the tetraspanin, CD9. We confirmed binding of PSG17 to CD9 by ELISA, flow cytometry, alkaline phosphatase binding assays, and in situ rosetting. Anti-CD9 monoclonal antibody inhibited binding of PSG17 to CD9-transfected cells and RAW 264.7 cells. Moreover, PSG17 binding to macrophages from CD9-deficient mice was significantly reduced. We then tested whether PSG17 binds to other members of the murine tetraspanin family. PSG17 did not bind to cells transfected with CD53, CD63, CD81, CD82, or CD151, suggesting that PSG17–CD9 binding is a specific interaction. We have identified the first receptor for a murine PSG as well as the first natural ligand for a member of the tetraspanin superfamily.

Key Words: tetraspanins • macrophages • expression cloning • placenta • PSG

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