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Arakawa, H. ; Kudo, H. ; Batrak, V. ; Caldwell, R.B. ; Rieger, M. ; Ellwart, J.W. ; Buerstedde, J.-M.

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

Nucleic Acids Res. 36:e1 (2008)
Verlagsversion Volltext DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter GREEN FLUORESCENT PROTEIN; IMMUNOGLOBULIN GENE CONVERSION; SOMATIC HYPERMUTATION; MOLECULAR EVOLUTION; CRYSTAL-STRUCTURE; MATURATION; RECOMBINATION; GENERATION; ANTIBODIES; MUTANTS
ISSN (print) / ISBN 0305-1048
e-ISSN 1362-4962
Zeitschrift Nucleic Acids Research
Quellenangaben Band: 36, Heft: 1, Seiten: , Artikelnummer: e1 Supplement: ,
Verlag Oxford University Press
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Stem Cell Research (ISF)
Translational Metabolic Oncology (IDC-TMO)
Institute of Molecular Immunology (IMI)
Institute of Molecular Radiation Biology (IMS)