Abstract
When monoclonal antibodies (mAbs) became available as an option for immunotherapy, it soon became evident that, apart from specificity and affinity, the isotype of the mAb was important for its effectiveness. Different isotypes of murine (m) immunoglobulin exhibited significant differences in their capability to interact with human effector systems. Differences in their binding to human Fc receptors for IgG (Fcy receptors) were especially prominent. Human monocytes could perform antibody-dependent cellular cytotoxicity (ADCC) against tumour cells in the presence of murine IgG2a mAB, but only slightly or not at all with the mIgG1 or mIgG2b subclasses 1. Subsequently, it was shown that monomeric mIgG2a (and mIgG3) could bind to human monocyte Fc receptors whereas no binding occured with monomeric mIgG1 or mIgG2b 2.
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