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* Department of Veterinary Microbiology and Pathology, Washington State University, Pullman;
Department of Biomedical Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Japan;
Benoaroya Research Institute, Virginia Mason Research Center, Seattle, Washington;
Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey; and
|| Department of Veterinary Microbiology, Seoul National University, Korea
Correspondence: W. C. Davis, Department of Veterinary Microbiology and Pathology College of Veterinary Medicine, Bustad Hall, Room 326, Washington State University, Pullman, WA 99164-7040. E-mail: davisw{at}mail.vetmed.wsu.edu
Workshop cluster 1 (WC1) is a member of the scavenger receptor cysteine-rich (SRCR) superfamily that includes CD5, CD6, CD163, and M160. Bovine WC1 consists of 11 SRCR domains, a unique domain 1, and two homologous 5 SRCR domain cassettes, WC1 domains 2–6 and 7–11. The porcine orthologue of WC1 contains five SRCR domains with a different domain arrangement. Although the function of WC1 is unknown, WC1 is proposed to be an accessory or homing molecule. Thus, identification of cells that express the counter receptor for WC1 (WC1-CR) is critical to understanding the function of WC1. For this reason, we constructed WC1-human immunoglobulin G1 fusion proteins to identify the binding domain of WC1 and cells that express the WC1-CR. Immunohistochemical analysis revealed WC1 domains 9 and 11 bind cells with macrophage and dendritic cell morphology and cells in ellipsoids in the spleen. These results and the finding of conserved signaling motifs in the cytoplasmic tail suggest WC1 may be an accessory molecule.
Key Words: bovine • 
T lymphocytes • cell surface molecule • immunohistochemistry
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