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Updated: May 20, 2026
08:58
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Pathological crystallization of human immunoglobulins
Ying Wang1, Aleksey Lomakin, Teru Hideshima
1Materials Processing Center, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. g09@mit.edu
Summary
Monoclonal immunoglobulin G (IgG) cryoglobulins from multiple myeloma patients form crystals and show varied condensation. This suggests immunoglobulin precipitation is possible even during common immune responses.
Area of Science:
- Biochemistry
- Immunology
- Crystallography
Background:
- Immunoglobulin (Ig) condensation is observed in pharmaceutical formulations and in vivo, notably in cryoglobulinemia.
- Monoclonal IgG cryoglobulins are associated with certain hematological disorders.
Purpose of the Study:
- To investigate the condensation and crystallization behavior of monoclonal IgG cryoglobulins.
- To correlate observed condensate morphologies with clinical findings.
Main Methods:
- Studied monoclonal IgG cryoglobulins from two multiple myeloma patients.
- Measured solubility lines of the cryoglobulins.
- Observed condensate morphologies under varying supersaturation conditions.
Main Results:
- The monoclonal IgG cryoglobulins formed crystals with diverse morphologies.
- Condensate morphologies were consistent with those reported in clinical cryoglobulinemia.
- Crystallization occurred at surprisingly low concentrations.
Conclusions:
- Monoclonal IgG cryoglobulins exhibit distinct crystallization and condensation behaviors.
- Observed phenomena provide insights into cryoglobulin formation in multiple myeloma.
- The study suggests that Ig precipitation may occur during regular immune responses, not just in pathological conditions.
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