IgE glycosylation and impact on structure and function: A systematic review

Area of Science:

• Immunology
• Glycobiology
• Molecular Biology

Background:

• Human immunoglobulin E (IgE) glycosylation's role in structure, function, and disease is not fully understood.
• Existing reviews focus on specific aspects like disease association or FcεR binding.
• Heterogeneity in studies complicates drawing definitive conclusions.

Purpose of the Study:

• To conduct the first systematic review of human IgE glycosylation using PRISMA guidelines.
• To establish a consensus on the roles of glycosylation in IgE structure, biology, and disease.
• To identify potential therapeutic targets related to IgE glycosylation.

Main Methods:

• Systematic literature review adhering to PRISMA guidelines.
• Analysis of diverse studies on human IgE glycosylation.
• Synthesis of evidence regarding glycosylation's impact on IgE structure and function.

Main Results:

• Evidence suggests differential IgE glycosylation profiles in allergic diseases versus healthy states.
• Glycosylation impacts IgE function, contributing to hypersensitivities and atopic diseases.
• Specific glycan sites (e.g., N394) and terminal structures (e.g., sialic acid) influence IgE structure, metabolism, and FcεR interactions.

Conclusions:

• Human IgE glycosylation plays a critical role in health and disease, especially in allergic conditions.
• Altered glycosylation impacts IgE structure, FcεR binding, and overall function.
• Further research with novel analytics is needed to explore IgE glycosylation for therapeutic strategies.