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Human polyreactive and monoreactive antibodies: effect of glycosylation antigen binding |
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| Authors: | Donadel Giulia; Calabro Anthony; Sigounas George; Hascall Vincent C; Notkins Abner Louis; Harindranath Nagaradona |
| Institution: | 1Laboratory of Oral Medicine, National Institute of Dental Research, National Institutes of Health Bethesda, MD 20892, USA 2Bone Research Branch, National Institute of Dental Research, National Institutes of Health Bethesda, MD 20892, USA 3Present address: Center for Biologics Evaluation and Research, Food and Drug Administration Building 29A, Room 2B09, Bethesda, MD 20892, USA |
| Abstract: | The present experiments were initiated to determine whetherthe carbohydrate portions of antibody molecules contribute topolyreactivity. Cell lines making human monoclonal polyreactiveor monoreactive antibodies of the immunoglobulin (Ig) M, IgGand IgA isotypes were treated with tunicamycin to block N-linkedglycosylation of the proteins. Analysis of the secreted nativeand non-glycosylated proteins revealed a >95% inhibitionof 3H]mannose incorporation. Electrophoresis on sodium dodecylsulphate-polyacrylamide gels of the proteins from tunicamycin-treatedcells showed increased mobility and the absence of 3H]mannoseincorporation of the immunoglobulin heavy chains, consistentwith the lack of glycosylation. The native and non-glycosylatedantibodies were then tested for their ability to bind differentantigens. Despite the lack of glycosylation, both polyreactiveand monoreactive antibodies bound to antigens with little ifany loss of reactivity or specificity. It is concluded thatthe carbohydrate moieties do not contribute significantly topolyreactivity. antigen binding glycosylation polyreactive antibodies |
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