Final answer:
Two mutational mechanisms that enhance antibody effectiveness are affinity maturation, which optimizes antibody-antigen binding, and the humanization of monoclonal antibodies, which reduces their immunogenicity. Additionally, the development of plantibodies through genetic engineering of plants could reduce therapy costs and improve accessibility.
Step-by-step explanation:
There are several mutational mechanisms that can improve the effectiveness of antibodies (Abs) produced within the body. One key mechanism is affinity maturation. When an animal is injected with an antigen for the second time, affinity maturation takes place, enhancing the affinity with which antibodies bind to their specific antigen, thus increasing their effectiveness. This occurs through somatic hypermutation in the variable regions of immunoglobulin genes, leading to the selection of B cells that produce higher-affinity antibodies.
Another mechanism is the development of humanized monoclonal antibodies (mAbs) for clinical use, such as rituximab, cetuximab, and trastuzumab. These humanized mAbs minimize the immune response against the therapy when used in humans. In humanization, the mouse constant region DNA of the antibody is replaced with human constant region DNA, reducing the immunogenicity of these therapeutic antibodies.
In addition, advancements in biotechnology have allowed for the cloning of antibody genes into plants, leading to the production of plantibodies. This innovation has the potential to significantly reduce production costs and facilitate oral delivery of antibodies through consumption of the engineered plants, thus simplifying the provision of immunotherapy in regions with limited healthcare infrastructure.