N-glycosylation is required for human CD2 immunoadhesion functions
| Autor: | M A, Recny, M A, Luther, M H, Knoppers, E A, Neidhardt, S S, Khandekar, M F, Concino, P A, Schimke, M A, Francis, U, Moebius, B B, Reinhold |
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| Rok vydání: | 1992 |
| Předmět: |
Antigens
Differentiation T-Lymphocyte Glycosylation Membrane Glycoproteins Rosette Formation Base Sequence Molecular Sequence Data CD2 Antigens CD58 Antigens Mass Spectrometry Structure-Activity Relationship Oligodeoxyribonucleotides Antigens CD Mutagenesis Site-Directed Humans Amino Acid Sequence Receptors Immunologic Cell Adhesion Molecules |
| Zdroj: | The Journal of biological chemistry. 267(31) |
| ISSN: | 0021-9258 |
| Popis: | The T-lymphocyte glycoprotein receptor, CD2, mediates cell-cell adhesion by binding to the surface molecule CD58 (LFA-3) on many cell types including antigen presenting cells. Two domains comprise the CD2 extracellular segment, with all adhesion functions localized to the amino-terminal domain that contains a single N-glycosylation site at Asn65. We have defined an important role for the N-linked glycans attached to Asn65 of this domain in mediating CD2-CD58 interactions and also characterize its N-glycotype structure. Analysis of deglycosylated soluble recombinant CD2 as well as a mutant transmembrane CD2 molecule containing a single Asn65-Gln65 substitution demonstrates that neither deglycosylated CD2 nor the mutant CD2 transmembrane receptor binds CD58 or monoclonal antibodies directed at native CD2 adhesion domain epitopes. Electrospray ionization-mass spectrometry demonstrates that high mannose oligosaccharides ((Man)nGlcNAc2, n = 5-9) are the only N-glycotypes occupying Asn65 when soluble CD2 is expressed in Chinese hamster ovary cells. Based on a model of human CD2 secondary structure, we propose that N-glycosylation is required for stabilizing domain 1 in the human receptor. Thus, N-glycosylation is essential for human CD2 adhesion functions. |
| Databáze: | OpenAIRE |
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