Serum antibody screening using glycan arrays

Marglous, Samantha; Brown, Claire E.; Padler-Karavani, Vered; Cummings, Richard D.; Gildersleeve, Jeffrey C.

doi:10.1039/d3cs00693j

Chem. Soc. Rev.

2024

DOI: 10.1039/d3cs00693j

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Serum antibody screening using glycan arrays

Samantha Marglous,

Claire E. Brown,

Vered Padler-Karavani

et al.

Abstract: Glycan microarrays provide a high-throughput platform to rapidly interrogate serum anti-glycan antibodies, identify new biomarkers for a variety of conditions, and analyze the immune system's response to vaccines and other treatments.

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2024

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Cited by 3 publications

References 324 publications

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Insights into Glycobiology and the Protein-Glycan Interactome Using Glycan Microarray Technologies

Heimburg-Molinaro,

Mehta,

Tilton

et al. 2024

Molecular & Cellular Proteomics

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Insights into Glycobiology and the Protein-Glycan Interactome Using Glycan Microarray Technologies

Heimburg-Molinaro,

Mehta,

Tilton

et al. 2024

Molecular & Cellular Proteomics

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O-glycosylation of IgA1 and the pathogenesis of an autoimmune disease IgA nephropathy

Novak,

King,

Yother

et al. 2024

Glycobiology

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IgA nephropathy is a kidney disease characterized by deposition of immune complexes containing abnormally O-glycosylated IgA1 in the glomeruli. Specifically, some O-glycans are missing galactose that is normally β1,3-linked to N-acetylgalactosamine of the core 1 glycans. These galactose-deficient IgA1 glycoforms are produced by IgA1-secreting cells due to a dysregulated expression and activity of several glycosyltransferases. Galactose-deficient IgA1 in the circulation of patients with IgA nephropathy is bound by IgG autoantibodies and the resultant immune complexes can contain additional proteins, such as complement C3. These complexes, if not removed from the circulation, can enter the glomerular mesangium, activate the resident mesangial cells, and induce glomerular injury. In this review, we briefly summarize clinical and pathological features of IgA nephropathy, review normal and aberrant IgA1 O-glycosylation pathways, and discuss the origins and potential significance of natural anti-glycan antibodies, namely those recognizing N-acetylgalactosamine. We also discuss the features of autoantibodies specific for galactose-deficient IgA1 and the characteristics of pathogenic immune complexes containing IgA1 and IgG. In IgA nephropathy, kidneys are injured by IgA1-containing immune complexes as innocent bystanders. Most patients with IgA nephropathy progress to kidney failure and require dialysis or transplantation. Moreover, most patients after transplantation experience a recurrent disease. Thus, a better understanding of the pathogenetic mechanisms is needed to develop new disease-specific treatments.

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Broad-Spectrum Legionaminic Acid-Specific Antibodies in Pooled Human IgGs Revealed by Glycan Microarrays with Chemoenzymatically Synthesized Nonulosonosides

Kooner,

Yu,

Leviatan Ben-Arye

et al. 2024

Molecules

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The presence and the level of antibodies in human sera against bacterial glycans are indications of prior encounters with similar antigens and/or the bacteria that express them by the immune system. An increasing number of pathogenic bacteria that cause human diseases have been shown to express polysaccharides containing a bacterial nonulosonic acid called 5,7-di-N-acetyllegionaminic acid (Leg5,7Ac2). To investigate the immune recognition of Leg5,7Ac2, which is critical for the fight against bacterial infections, a highly effective chemoenzymatic synthon strategy was applied to construct a library of α2–3/6-linked Leg5,7Ac2-glycans via their diazido-derivatives (Leg5,7diN3-glycans) formed by efficient one-pot three-enzyme (OP3E) synthetic systems from a diazido-derivative of a six-carbon monosaccharide precursor. Glycan microarray studies using this synthetic library of a Leg5,7Ac2-capped collection of diverse underlying glycan carriers and their matched sialoside counterparts revealed specific recognition of Leg5,7Ac2 by human IgG antibodies pooled from thousands of healthy donors (IVIG), suggesting prior human encounters with Leg5,7Ac2-expressing pathogenic bacteria at the population level. These biologically relevant Leg5,7Ac2-glycans and their immune recognition assays are important tools to begin elucidating their biological roles, particularly in the context of infection and host–pathogen interactions.

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Serum antibody screening using glycan arrays

Abstract: Glycan microarrays provide a high-throughput platform to rapidly interrogate serum anti-glycan antibodies, identify new biomarkers for a variety of conditions, and analyze the immune system's response to vaccines and other treatments.

Cited by 3 publications

References 324 publications

Insights into Glycobiology and the Protein-Glycan Interactome Using Glycan Microarray Technologies

Insights into Glycobiology and the Protein-Glycan Interactome Using Glycan Microarray Technologies

O-glycosylation of IgA1 and the pathogenesis of an autoimmune disease IgA nephropathy

Broad-Spectrum Legionaminic Acid-Specific Antibodies in Pooled Human IgGs Revealed by Glycan Microarrays with Chemoenzymatically Synthesized Nonulosonosides

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