ArticleClinical proteomics2026
Pairing of high-mannose glycans in human IgE-Fc: implications for secretion and stability.
Article in Clinical proteomics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundImmunoglobulin E (IgE) is the least abundant antibody class in serum, but plays a central role in type I allergic responses. The Fc region of human IgE (IgE-Fc) contains four potential N-glycosylation sites: Asn265 and Asn371 are modified with complex-type glycans; Asn394 predominantly carries a high-mannose glycan; and Asn383 remains unmodified. Despite the recognized importance of glycosylation in antibody function, the structure-function relationships of the individual IgE-Fc glycans remain poorly understood. This study aimed to elucidate the structural and functional significance of N-glycans on IgE-Fc, particularly the high-mannose glycan attached to Asn394.
methodsThe expression and secretion of recombinant human IgE-Fc constructs including wild-type IgE-Fc, a high-mannose-deficient mutant (N394Q), and a triple mutant lacking complex-type glycans (N265Q/N371Q/N383Q) was assessed in mammalian Expi293F cells. In addition, the thermal stability of wild-type IgE-Fc treated with Endo H or PNGase F was evaluated by a thermal shift assay. Glycan compositions and pairing patterns in IgE-Fc were characterized by intact mass spectrometry (MS) and liquid chromatography-MS analysis of released glycans.
resultsWild-type IgE-Fc and the triple mutant were stably expressed, whereas secretion of the high-mannose-deficient mutant (N394Q) was markedly impaired, demonstrating that the Asn394 glycan is essential for proper folding and efficient secretion. Endo H treatment significantly decreased the melting temperature of wild-type IgE-Fc, indicating that high-mannose glycans contribute to structural stability. Integration of MS data on the intact protein and LC-MS data on the enzyme-released N-glycans revealed that high-mannose glycans at Asn394 associate in a non-selective manner between heavy chains.
conclusionsThese findings establish that the high-mannose glycan at Asn394 is required for both the secretion and structural stability of IgE-Fc. Furthermore, the observation of non-selective glycan pairing between heavy chains provides insight into the temporal coordination of disulfide bond formation and N-glycan processing during IgE biosynthesis, thereby advancing our understanding of the molecular mechanisms underlying IgE structure and function.
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