ABSTRACT
The original and dominant method for cloning murine monoclonal antibodies is through the fusion of antibody-producing spleen B cells and a myeloma line. In 1975, G. Kohler and C. Milstein showed that mouse myeloma cells could be fused to B lymphocytes from immunized mice resulting in continuously growing, specific monoclonal antibody-secreting somatic cell hybrids, or hybridoma cells. Phage display of antibody fragments is accomplished by coupling of the antibody fragment to a coat protein of the bacteriophage. The production of soluble antibody fragments from selected phages can be accomplished without subcloning. Bacterial Expression Early attempts to express intact antibody molecules in bacteria were fairly unsuccessful. The domain structure of the antibody molecule allows the reshuffling of domains and the construction of functional antibody fragments. Antibody fusion proteins are made by replacing a part of the antibody molecule with a fusion partner such as an enzyme or a toxin that confers a novel function to the antibody.
