Abstract
The CD85 molecule was originally defined at the Fifth Workshop on Leucocyte Antigens in 1993 by two monoclonal antibodies, VMP55 and GHI/75. This cell-surface glycoprotein is expressed on B cells, monocytes, and subpopulations of T and natural killer (NK) cells, and particularly high levels are expressed by normal and neoplastic plasma cells and by hairy cell leukemia B cells. We affinity purified the CD85 antigen and obtained tryptic peptide sequence which indicated that this molecule might be ILT2, a recently described inhibitory major histocompatibility complex class I receptor of the immunoglobulin superfamily. This was confirmed by showing that both of the original anti-CD85 mAbs stained ILT2 transfectants. The cell signaling role demonstrated for ILT2 is consistent with the previously reported involvement of CD85 in T cell activation.
| Original language | English |
|---|---|
| Pages (from-to) | 841-845 |
| Number of pages | 5 |
| Journal | Journal of Leukocyte Biology |
| Volume | 65 |
| Issue number | 6 |
| DOIs | |
| State | Published - 1999 |
Keywords
- B lymphocytes
- Monoclonal antibodies
- Signal transduction
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