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Human IgG2 antibodies display disulfide-mediated structural isoforms
Jette Wypych1, Ming Li, Amy Guo
1Department of Analytical Sciences, Amgen Inc., Thousand Oaks, California 91320, USA. jwypych@amgen.com
The Journal of Biological Chemistry
|March 15, 2008
Summary
Human immunoglobulin G2 (IgG2) molecules exhibit previously undiscovered structural diversity. Analysis reveals three distinct covalent structures (IgG2-A, -B, and -A/B) due to novel disulfide bonding patterns in antibodies.
Area of Science:
- Immunology
- Structural Biology
- Biochemistry
Background:
- Human immunoglobulin G2 (IgG2) is a crucial antibody subclass.
- The established covalent structure of IgG2 has been widely accepted.
- Previous studies have not fully characterized the disulfide bond heterogeneity in IgG2.
Purpose of the Study:
- To investigate the covalent structure of human IgG2 molecules.
- To identify and characterize novel structural isoforms of human IgG2.
- To understand the implications of disulfide bond variations in IgG2 structure.
Main Methods:
- Detailed analysis of recombinant human IgG2 monoclonal antibody.
- Characterization of disulfide bond structures.
- Comparison of novel structures with existing literature.
Main Results:
- Human IgG2 antibodies can be resolved into distinct structural forms based on disulfide bonds.
- Three main structural types were identified: IgG2-A (classic), IgG2-B (symmetrical complex), and IgG2-A/B (intermediate).
- Novel isoforms involve covalent linkages between light chain constant domain, heavy chain C(H)1 domain, and the hinge region.
Conclusions:
- Disulfide structural heterogeneity is a natural feature of human IgG2 subclass.
- These novel isoforms are present in native IgG2 from myeloma plasma and normal serum.
- The structural variations occur with both kappa and lambda light chains, albeit with differing ratios.
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