Serum and Plasma Immunoglobulin G Fc N-Glycosylation Is Stable during Storage

Immunoglobulin G (IgG) glycosylation is studied in biological samples to develop clinical markers for precision medicine, for example, in autoimmune diseases and oncology. Inappropriate storage of proteins, lipids, or metabolites can lead to degradation or modification of biomolecular features, which can have a strong negative impact on accuracy and precision of clinical omics studies. Regarding the preservation of IgG glycosylation, the range of appropriate storage conditions and time frame is understudied. Therefore, we investigated the effect of storage on IgG Fc N-glycosylation in the commonly analyzed biofluids, serum and plasma. Short-term storage and accelerated storage stability were tested by incubating samples from three healthy donors under stress conditions of up to 50 degrees C for 2 weeks using -80 degrees C for 2 weeks as the reference condition. All tested IgG glycosylation features-sialylation, galactosylation, bisection, and fucosylation-remained unchanged up to room temperature as well as during multiple freeze-thaw cycles and exposure to light. Only when subjected to 37 degrees C or 50 degrees C for 2 weeks, galactosylation and sialylation subtly changed. Therefore, clinical IgG glycosylation analysis does not rely as heavily on mild serum and plasma storage conditions and timely analysis as many other omics analyses.

Automated summary

The study focused on the effect of storage on IgG Fc N-glycosylation in serum and plasma samples, finding that most glycosylation features remain stable under normal storage conditions, with only minor changes observed under extreme heat stress conditions. The research suggests that clinical IgG glycosylation analysis may not be as sensitive to storage conditions and timing as other omics studies.