Serologic cross-reactivity of T11 target structure and lymphocyte function-associated antigen 3. Evidence for structural homology of the sheep and human ligands of CD2.
T11 target structure (T11TS) and lymphocyte function-associated antigen (LFA) 3 are the cell-surface glycoproteins on sheep and human erythrocytes (E) binding to cluster differentiation 2 (the E-receptor) on T cells in E rosette formation. Here we show that this functional cross-reactivity is most l...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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1987
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| _version_ | 1797080515417735168 |
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| author | Tiefenthaler, G Dustin, M Springer, T Hünig, T |
| author_facet | Tiefenthaler, G Dustin, M Springer, T Hünig, T |
| author_sort | Tiefenthaler, G |
| collection | OXFORD |
| description | T11 target structure (T11TS) and lymphocyte function-associated antigen (LFA) 3 are the cell-surface glycoproteins on sheep and human erythrocytes (E) binding to cluster differentiation 2 (the E-receptor) on T cells in E rosette formation. Here we show that this functional cross-reactivity is most likely due to a structural homology of these molecules. A rabbit antiserum to sheep T11TS is shown to cross-react with LFA-3 in several independent assays: (a) rabbit anti-T11TS antiserum blocks the formation of E rosettes by human T cells with both autologous and xenogeneic (sheep) E by binding to the respective E; (b) the antiserum blocks the binding of anti-LFA-3 monoclonal antibody to human E; and (c) it reacts with purified LFA-3 in Western blotting. Together, these findings demonstrate that T11TS on sheep E and LFA-3 on human E are serologically related, providing further support for the notion that T11TS and LFA-3 are the sheep and human forms of the same cell interaction molecule. |
| first_indexed | 2024-03-07T01:01:13Z |
| format | Journal article |
| id | oxford-uuid:89cdb73b-6a37-4ae3-929e-0375fc4d0fd4 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:01:13Z |
| publishDate | 1987 |
| record_format | dspace |
| spelling | oxford-uuid:89cdb73b-6a37-4ae3-929e-0375fc4d0fd42022-03-26T22:27:00ZSerologic cross-reactivity of T11 target structure and lymphocyte function-associated antigen 3. Evidence for structural homology of the sheep and human ligands of CD2.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:89cdb73b-6a37-4ae3-929e-0375fc4d0fd4EnglishSymplectic Elements at Oxford1987Tiefenthaler, GDustin, MSpringer, THünig, TT11 target structure (T11TS) and lymphocyte function-associated antigen (LFA) 3 are the cell-surface glycoproteins on sheep and human erythrocytes (E) binding to cluster differentiation 2 (the E-receptor) on T cells in E rosette formation. Here we show that this functional cross-reactivity is most likely due to a structural homology of these molecules. A rabbit antiserum to sheep T11TS is shown to cross-react with LFA-3 in several independent assays: (a) rabbit anti-T11TS antiserum blocks the formation of E rosettes by human T cells with both autologous and xenogeneic (sheep) E by binding to the respective E; (b) the antiserum blocks the binding of anti-LFA-3 monoclonal antibody to human E; and (c) it reacts with purified LFA-3 in Western blotting. Together, these findings demonstrate that T11TS on sheep E and LFA-3 on human E are serologically related, providing further support for the notion that T11TS and LFA-3 are the sheep and human forms of the same cell interaction molecule. |
| spellingShingle | Tiefenthaler, G Dustin, M Springer, T Hünig, T Serologic cross-reactivity of T11 target structure and lymphocyte function-associated antigen 3. Evidence for structural homology of the sheep and human ligands of CD2. |
| title | Serologic cross-reactivity of T11 target structure and lymphocyte function-associated antigen 3. Evidence for structural homology of the sheep and human ligands of CD2. |
| title_full | Serologic cross-reactivity of T11 target structure and lymphocyte function-associated antigen 3. Evidence for structural homology of the sheep and human ligands of CD2. |
| title_fullStr | Serologic cross-reactivity of T11 target structure and lymphocyte function-associated antigen 3. Evidence for structural homology of the sheep and human ligands of CD2. |
| title_full_unstemmed | Serologic cross-reactivity of T11 target structure and lymphocyte function-associated antigen 3. Evidence for structural homology of the sheep and human ligands of CD2. |
| title_short | Serologic cross-reactivity of T11 target structure and lymphocyte function-associated antigen 3. Evidence for structural homology of the sheep and human ligands of CD2. |
| title_sort | serologic cross reactivity of t11 target structure and lymphocyte function associated antigen 3 evidence for structural homology of the sheep and human ligands of cd2 |
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