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Start Over Author "Diana Liu" Journal biochemistry
2 results on '"Diana Liu"'

1. Interchain disulfide bonding in human IgG2 antibodies probed by site-directed mutagenesis

Author

Allen, Martin J., Amy Guo, Martinez, Theresa, Mei Han, Flynn, Gregory C., Wypych, Jette, Yaoqing Diana Liu, Shen, Wenyan D., Dillon, Thomas M., Vezina, Christopher, and Balland, Alain

Subjects
Immunoglobulin G -- Chemical properties, Immunoglobulin G -- Structure, Mutagenesis -- Analysis, Sulfides -- Chemical properties, Sulfides -- Structure, Biological sciences, Chemistry
Abstract

Several studies are conducted to explain the interchain disulfide bonding preset in the human IgG2 antibodies. The results demonstrate that a reduction in the sulfide bond heterogeneity in these antibodies while preserving their activities can be easily obtained by the application of site-directed mutagenesis.

Published
2009

2. Interchain Disulfide Bonding in Human IgG2 Antibodies Probed by Site-Directed Mutagenesis

Author

Gregory C. Flynn, Yaoqing Diana Liu, Jette Wypych, Theresa Martinez, Mei Han, Thomas M. Dillon, Martin J. Allen, Christopher J. Vezina, Alain Balland, Amy Guo, and Wenyan D Shen

Subjects
Spectrometry, Mass, Electrospray Ionization, medicine.drug_class, Ion chromatography, Monoclonal antibody, Peptide Mapping, Biochemistry, Immunoglobulin kappa-Chains, chemistry.chemical_compound, Serine, medicine, Humans, Cysteine, Disulfides, Sodium dodecyl sulfate, Site-directed mutagenesis, Polyacrylamide gel electrophoresis, Cysteine metabolism, Mutagenesis, Antibodies, Monoclonal, Peptide Fragments, Recombinant Proteins, Amino Acid Substitution, chemistry, Immunoglobulin G, Mutagenesis, Site-Directed, Electrophoresis, Polyacrylamide Gel
Abstract

Human IgG2 exists as a mixture of disulfide-linked structural isoforms that can show different activities. To probe the contribution of specific cysteine residues to the formation of structural isoforms, we characterized a series of Cys-->Ser mutant IgG2 recombinant monoclonal antibodies, focused on the first C(H)1 cysteine and the first two hinge cysteines. These residues participate in the formation of structural isoforms that have been noted by nonreduced capillary sodium dodecyl sulfate polyacrylamide gel electrophoresis, reversed-phase high-performance liquid chromatography, and cation exchange chromatography. We show that single Cys-->Ser mutants can greatly reduce heterogeneous disulfide bonding in human IgG2 and maintain in vitro activity. The data demonstrate the feasibility of applying site-directed mutagenesis to reduce disulfide bond heterogeneity in human IgG2 while preserving the activity of this therapeutically important class of human antibodies.

Published
2009

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