Brief Report

Oligomeric forms of single chain immunoglobulin (scIgG)

Volume 2, Issue 1   January/February 2010
Pages 73 - 76
http://dx.doi.org/10.4161/mabs.2.1.10784
Thomas Schirrmann, Christian Menzel, Michael Hust, Jessica Prilop, Thomas Jostock and Stefan Dübel

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Assembly of immunoglobulin G (IgG) molecules from two heavy and two light chains can be facilitated by connecting the light chain to the heavy chain by an oligopeptide linker. Production of the anti-lysozyme D1.3-single chain (sc) IgG1 in HEK293T cells yielded up to 8 mg/L functional scIgG polypeptide. Size exclusion chromatography of material purified by protein-A affinity chromatography revealed that the majority of the D1.3-scIgG1 molecules were 150kDa monomers, with a KD of 1.8x10-10M measured by surface plasmon resonance; however, significant fractions of scIgG dimers and oligomers with molecular masses of 300 kDa and >600 kDa, respectively, were identified. The oligomerization resulted in an increased avidity. The observed oligomerization capability may allow new approaches for the generation of bispecific / multivalent antibodies.

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