| First Author | Daniels BF | Year | 1994 |
| Journal | Immunity | Volume | 1 |
| Issue | 9 | Pages | 785-92 |
| PubMed ID | 7895167 | Mgi Jnum | J:189421 |
| Mgi Id | MGI:5445498 | Doi | 10.1016/s1074-7613(94)80020-0 |
| Citation | Daniels BF, et al. (1994) Ly-49A, a receptor for H-2Dd, has a functional carbohydrate recognition domain. Immunity 1(9):785-92 |
| abstractText | Ly-49A+ murine natural killer (NK) cells cannot lyse target cells that express H-2Dd. We demonstrate a functional requirement for carbohydrate recognition by Ly-49A. Treatment of H-2Dd+ target cells with tunicamycin prevents their binding to Ly-49A+ cells and renders them susceptible to lysis by Ly-49A+ NK cells. Fucoidan, a sulfated polysaccharide, binds to Ly-49A in a calcium-dependent manner, and this binding is inhibited by monosaccharides, particularly sulfated hexoses. The inactivation of Ly-49A+ NK cells by H-2Dd+ target cells is reversed in the presence of glucose 6-SO4. These results indicate that Ly-49A has a functional carbohydrate recognition domain and that target expression of carbohydrates alters their susceptibility to natural killing. |
