Introduciton: Unlike monoclonal antibodies from hybridomas, recombinant antibodies from bacteria usually suffer from poor stability and yield. Due to surface displayed antibody molecules, recombinant antibodies are easily screened, though. (WP1) In order to combine both advantages, we plan to construct a library of >10(+6) different hybridomas by consecutive homologous and specific recombinations, with all of the hybridomas descending from one single cell. Each dell displays >100.000 of "its" specifi c antibody molecules on the cell surface. Therefore, the library should be easily screened fo low to medium affinity human antibodies specific for almost all antigens. (WP2) Antibodies of higher affinities will be generated by the apparatus responsible fo r somatic hypermutations currently being deciphered, whereby FACS-screening offers an especially easy method to compare affinities. (WP3) The ancestor cell line of our antibody library is engineered to emit signals in response to antigen binding, thus a llowing for the labelling detection of antigen-specific antibodies. Outlook: The combined efforts described above might evolve into a method that supersedes the current state of the art in the production of monoclonal antibodies.
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