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Immunogenicity of non-human proteins such as plant derived toxin molecules and bacterial enzymes provide an almost complete barrier to their clinical implementation as novel therapeutic strategies for cancer. It is also recognised that the immunogenicity associated with therapeutic antibodies and certain human proteins can also limit their clinical effectiveness. For therapeutic antibodies a number of engineering options exist, and clearly have in part been developed to address the issue of immunogenicity. Examples include "classic" humanisation by CDR engraftment, use of human Ig libraries such as phage display systems and human Ig transgenic mice. However, in each case there should be an expectation that these can all result in antibodies still capable of eliciting an immune response in certain patients. This is connected to the process of affinity maturation during antibody generation that inevitably results in antibodies to which patients may not be naturally tolerant. Underlying this process is the presentation of T-helper peptide epitopes derived from the intracellular processing of the therapeutic antibody. Foreign T-cell epitopes are also present in plant toxins and bacterial enzymes and will cause a sustained immune response and the generation of immunological memory.

Limiting the risk of immunogenicity by identification and removal of T-cell epitopes (DeImmunisation™)