Cutting Edge: Identification of GL50, a Novel B7-Like Protein That Functionally Binds to ICOS Receptor

Vincent Ling(Institute of Immunology), Paul W. Wu(Institute of Immunology), Heather Finnerty(Institute of Immunology), Kevin M. Bean(Institute of Immunology), Vicki Spaulding(Institute of Immunology), Lynette A. Fouser(Institute of Immunology), John P. Leonard(Institute of Immunology), Sharon Hunter(Institute of Immunology), Richard Zollner(Institute of Immunology), Jenifer L. Thomas(Institute of Immunology), Joy Miyashiro(Institute of Immunology), Kenneth Jacobs(Institute of Immunology), Mary Collins(Institute of Immunology)
The Journal of Immunology
February 1, 2000
Cited by 231Open Access
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Abstract

Abstract By the genetic selection of mouse cDNAs encoding secreted proteins, a B7-like cDNA clone termed mouse GL50 (mGL50) was isolated encoding a 322-aa polypeptide identical with B7h. Isolation of the human ortholog of this cDNA (hGL50) revealed a coding sequence of 309 aa residues with 42% sequence identity with mGL50. Northern analysis indicated GL50 to be present in many tissues including lymphoid, embryonic yolk sac, and fetal liver samples. Of the CD28, CTLA4, and ICOS fusion constructs tested, flow cytometric analysis demonstrated only mouse ICOS-IgG binding to mGL50 cell transfectants. Subsequent phenotyping demonstrated high levels of ICOS ligand staining on splenic CD19+ B cells and low levels on CD3+ T cells. These results indicate that GL50 is a specific ligand for the ICOS receptor and suggest that the GL50-ICOS interaction functions in lymphocyte costimulation.


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