| Autor: |
Leader, K.A., Kumpel, B.M., Hadley, A.G., Bradley, B.A. |
| Předmět: |
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| Zdroj: |
Immunology; Apr91, Vol. 72 Issue 4, p481-485, 5p |
| Abstrakt: |
Four human monoclonal antibodies (mAb) to the Rh antigen D were produced in aglycosylated forms by culture of B-cell lines in medium containing tunicamycin (Tm-mAb). Erythrocytes sensitized with these or control mAb were compared in U937 rosette and monocyte chemiluminescence assays to determine Fey receptor I (FcγRI)-mediated functional activity, and in lymphocyte rosette and lymphocyte antibody-dependent cell-mediated cytotoxicity (ADCC) assays to study FcγyRIII-mediated binding and lysis. FcγRI-mediated interactions with Tm-mAb were greatly reduced compared with control mAb. All Tm-mAb failed to promote ADCC, although lymphocyte rosette formation was unaltered. The anti-D titre of Tm-mAb and their interaction with mAb JL512 (recognizing an epitope in the CH2 domain) were unchanged. These data suggest that glycosylation of IgG is required for CH2 domain interactions with both FcγRI and FcγRIII, but not for CH3 domain interactions with Fcγ, RIII. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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