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Evidence for Sulfate Modification of H-2D^d on N-Linked Carbohydrate(s): Possible Involvement in Ly-49A Interaction¹

Department of Medical Microbiology and Immunology, Faculty of Medicine, University of Alberta, Edmonton, Alberta, Canada

Murine class I molecules are ligands for Ly-49 molecules, a family of regulatory receptors expressed on murine NK cells. Since soluble sulfated mono- and polysaccharides interfere with the interaction of Ly-49A, a C-type lectin, and its class I ligand, D^d, it is possible that the oligosaccharides on class I molecules are sulfated and participate in Ly-49A binding. In this report, we show that H-2D^d expressed by activated T cells and various tumor cell lines is sulfated, as demonstrated by immunoprecipitation of D^d following Na₂³⁵SO₄ labeling. The ³⁵SO₄^-2 label on D^d expressed by a representative tumor cell, NZB1.1, is removed by peptide N-glycosidase F, but is resistant to endoglycosidase H treatment, indicating that the sulfate group is located on mature N-linked oligosaccharides. Two-dimensional SDS-PAGE analysis revealed that all major mature glycosylation variants of the D^d expressed by NZB1.1 are sulfated. Sodium chlorate, a potent inhibitor of ATP-sulfurylase, which prevents the formation of the sulfate donor, 3'-phosphoadenosine 5'-phosphosulfate, inhibited metabolic sulfation of D^d. NZB1.1 binds isolated Ly-49A immobilized on solid phase through an interaction by cell surface D^d, since cell adhesion was blocked by Abs directed against D^d or Ly-49A. Treatment of the D^d-expressing NZB1.1 tumor cells with sodium chlorate reduced their ability to bind immobilized Ly-49A, particularly when Ly-49A density was limiting. These results provide evidence for sulfation of H-2D^d oligosaccharide moieties, and suggest a role for this posttranslational modification in the interaction of D^d with Ly-49A.

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