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Lectin receptors on IgA isotypes

A E Wold¹, C Motas, C Svanborg

¹Institute of Biochemistry, Bucharest, Romania.

Scandinavian Journal of Immunology

|February 1, 1994

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Human IgA1 and IgA2 isotypes show distinct N-linked oligosaccharide profiles, influencing their interaction with lectins. These differences in lectin receptor activity may impact interactions with microbes and host receptors.

Area of Science:

Immunology
Glycobiology
Microbial Interactions

Background:

Secretory IgA (sIgA) interacts with mannose-specific lectins on Escherichia coli.
Human immunoglobulin A (IgA) exists as two main isotypes, IgA1 and IgA2.

Purpose of the Study:

To investigate differences in N-linked oligosaccharide chain lectin receptor activity between human IgA1 and IgA2.
To determine if these glycan differences affect IgA isotype interactions.

Main Methods:

Utilized a panel of plant lectins specific for N-linked oligosaccharides.
Tested lectin precipitation of IgA1 and IgA2 myeloma proteins, secretory IgA, and free secretory component.

Main Results:

IgA2 showed stronger reactivity than IgA1 with mannose-specific lectin Concanavalin A (ConA).

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IgA1 exhibited stronger binding than IgA2 to galactose-specific lectins (Ricinus communis agglutinin I, Abrus precatorius agglutinin).

IgA2 displayed greater reactivity than IgA1 with Lens culinaris (lentil) and Pisum sativum (pea) lectins, suggesting differences in core fucosylation and chain truncation.

Conclusions:

Human IgA1 and IgA2 isotypes possess distinct N-linked oligosaccharide structures.
These glycan variations influence lectin binding profiles, indicating differential receptor activity.
Observed differences may play a role in IgA isotype interactions with microbial flora and host lectin receptors, such as phagocyte receptors.