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

Hiroshi Arakawa | Zendy; Hisaaki Kudo | Zendy; Vera Batrak | Zendy; Randolph B. Caldwell | Zendy; Michael A. Rieger | Zendy; Joachim W. Ellwart | Zendy; Jean-Marie Buerstedde | Zendy

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

Author(s) -

Hiroshi Arakawa,

Hisaaki Kudo,

Vera Batrak,

Randolph B. Caldwell,

Michael A. Rieger,

Joachim W. Ellwart,

Jean-Marie Buerstedde

Publication year - 2007

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/gkm616

Subject(s) - somatic hypermutation , biology , cell sorting , transgene , gene conversion , genetics , gene , mutant , mutation , population , immunoglobulin gene , affinity maturation , antibody , microbiology and biotechnology , genome , b cell , cell , demography , sociology

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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