Bacterial expression of immunoglobulin fragments.
The expression of Ig fragments in Escherichia coli permits rapid access to engineered molecules with antigen-binding properties. While the expression in a functional state by secretion to the periplasm is the standard method for the production of Fv and Fab fragments, single chain Fv fragments are mainly produced by refolding from insoluble aggregates. Although all of these Ig fragments serve as valuable aids in the study of antigen binding, their different biochemical properties must be considered when using them as research tools or for medical applications. In addition to these simple univalent antibody fragments, the bacterial expression of bivalent and bispecific versions and of hybrid proteins with novel effector functions is gaining increasing importance.
Skerra
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Max-Planck-Institut für Biophysik, Frankfurt am Main, Germany.
D000818:Animals; D000918:Antibody Specificity; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000096:biosynthesis / Q000235:genetics; D007128:Immunoglobulin Fragments / Q000096:biosynthesis* / Q000235:genetics; D007135:Immunoglobulin Variable Region / Q000096:biosynthesis / Q000235:genetics; D051379:Mice; D015202:Protein Engineering; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis*
D007140:Immunoglobulin Fab Fragments; D007128:Immunoglobulin Fragments; D007135:Immunoglobulin Variable Region; D011993:Recombinant Fusion Proteins