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Comparative HILIC-UPLC analysis of immunoglobulin G N-glycome from saliva and plasma

Immunoglobulin G (IgG) is the most abundant antibody in the blood and plays a critical role in host immune defence against infectious pathogens. IgG glycosylation is known to modulate IgG effector functions and is involved in the development and progression of disease. Because the reactivity of salivary IgG mirrors that of plasma IgG, saliva is an attractive alternative to blood for studies in which antibody analysis is intended to provide an indication of a subject's immune status. Therefore, in this study, we described a rapid and effective method for comparative N-glycome analysis of IgG from human plasma and saliva samples. Plasma and saliva were collected from 9 healthy volunteers within a 2- hour time window. IgGs were affinity-purified from the two biofluids with protein G-agarose beads and then denatured and enzymatically deglycosylated. The released N-glycans were analysed by ultra-high performance liquid chromatography with hydrophilic interaction analysis (HILIC-UPLC). IgG from saliva exhibited reduced galactosylation and sialylation compared with IgG from plasma, whereas core fucosylation remained unchanged. The slightly proinflammatory profile of salivary IgG may be due to higher exposure to pathogens compared with plasma IgG. This study provides an additional tool for the analysis of salivary IgG glycosylation and highlights its potential as a surrogate biomarker for the study of plasma IgG.

N-glycosylation, immunoglobulin G, saliva, biomarker

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