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Protein evolution by hypermutation and selection in the B cell line DT40

Hiroshi Arakawa1, Hiroaki Kudo, Vera Batrak

  • 1Institute for Molecular Radiobiology, Institute of Stem Cell Research, GSF-National Research Center for Environment and Health, Ingolstaedter Landstrasse 1, D-85764 Neuherberg-Munich, Germany.

Nucleic Acids Research
|December 13, 2007
PubMed

Genome-wide mutations and selection within a population are the basis of natural evolution. A similar process occurs during antibody affinity maturation when immunoglobulin genes are hypermutated and only those B cells which express antibodies of improved antigen-binding specificity are expanded. Protein evolution might be simulated in cell culture, if transgene-specific hypermutation can be combined with the selection of cells carrying beneficial mutations. Here, we describe the optimization of a GFP transgene in the B cell line DT40 by hypermutation and iterative fluorescence activated cell sorting. Artificial evolution in DT40 offers unique advantages and may be easily adapted to other transgenes, if the selection for desirable mutations is feasible.

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