Role of siglecs and related glycan-binding proteins in immune responses and immunoregulation

Bochner, Bruce S.; Zimmermann, Nives

doi:10.1016/j.jaci.2014.11.031

Cited by 97 publications

(77 citation statements)

References 116 publications

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“…Not only proteins but also carbohydrates can stimulate the production of IgE antibodies and be strong inducers of 2 responses [33]. e current estimate is that 15-30 % of allergic patients generate speci c anti-carbohydrate IgE antibodies [34], but this IgE response has very little clinical relevance [35].…”

Section: Features Of the Immune Response To Carbohydratesmentioning

confidence: 99%

The red meat allergy syndrome in Sweden

Apostolović¹,

Tran²,

Starkhammar³

et al. 2016

Allergo J

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SummaryIn the last decade, a novel type of food allergy presenting with severe allergic reactions several hours a er consumption of red meat has been recognized.e allergic responses are due to IgE antibodies directed against the carbohydrate epitope galactose-α-1,3-galactose (α-Gal) found in mammalian meat.is review presents the red meat allergy syndrome in Sweden, discusses the features of the immune response to carbohydrates, and highlights the presence of heat stable α-Gal-containing proteins in meat.e number of diagnosed red meat allergy cases in Sweden has increased signi cantly over the past few years. All patients have been tick bitten. Our recent work has shown that α-Gal is present in the Euro pean tick Ixodes ricinus (I. ricinus), thus potentially explaining the strong association between anti-α-Gal IgE and tick bites, with development of red meat allergy as a secondary phenomenon. Further studies using immunoproteomics have identi ed novel α-Gal-containing meat proteins that bound IgE from red meat allergic patients. Four of these proteins were stable to thermal processing pointing to the fact that the allergenicity of red meat proteins is preserved in cooked meat. In keeping with the fact that the α-Gal epitope is structurally related to the blood group B antigen, a positive association with the B-negative blood groups among our red meat allergic patients was noted. A selective IgE reactivity to the pure carbohydrate moiety was observed when investigating the speci city of the α-Gal immune response. IgE from red meat allergic patients does not recognize the other major mammalian carbohydrate, N-glycolylneuraminic acid (Neu5Gc), also present in high amounts in red meat. Furthermore, neither common cross-reactive carbohydrate determinants (CCDs) from plants nor venoms are targets of the IgE response in these patients.Taken together, the α-Gal carbohydrate has shown to be a potentially clinically relevant allergen that should be taken into account in the diagnosis of food allergy. Many new ndings in the eld of red meat allergy have been obtained during the past years, but further e orts to understand the process of digestion, absorption, and delivery of α-Gal-containing molecules to the circulation are needed. e red meat allergy syndrome in Sweden. Allergo Cite this as

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Section: Features Of the Immune Response To Carbohydratesmentioning

confidence: 99%

The red meat allergy syndrome in Sweden

Apostolović¹,

Tran²,

Starkhammar³

et al. 2016

Allergo J

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“…This approach is still the most reliable method for obtaining detailed structural information about the protein-modifying carbohydrates as the protein-level heterogeneity, both in terms of site occupancy and the number of site-specific structures, represent exceptional challenges for analysis. However, information about protein and site-specific glycosylation is lost by this approach, so there is a growing need for routine glycopeptide analysis, as glycosylation has been implicated as a key player in cell-cell interactions, host/pathogen interactions, enzymatic processing, and even intracellular signaling (7)(8)(9)(10)(11)(12)(13). Studies have shown that glycosylation is species-, and tissuespecific, and can be altered by disease or physiological changes (14 -22).…”

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confidence: 99%

Tissue-Specific Glycosylation at the Glycopeptide Level

Medzihradszky

Kaasik

Chalkley

2015

Molecular & Cellular Proteomics

107

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This manuscript describes the enrichment and mass spectrometric analysis of intact glycopeptides from mouse liver, which yielded site-specific N-and O-glycosylation data for ϳ130 proteins. Incorporation of different sialic acid variants in both N-and O-linked glycans was observed, and the importance of using both collisional activation and electron transfer dissociation for glycopeptide analysis was illustrated. The N-glycan structures of predicted lysosomal, endoplasmic reticulum (ER), secreted and transmembrane proteins were compared. The data suggest that protein N-glycosylation differs depending on cellular location. The glycosylation patterns of several mouse liver and mouse brain glycopeptides were compared. Tissue-specific differences in glycosylation were observed between sites within the same protein: Some sites displayed a similar spectrum of glycan structures in both tissues, whereas for others no overlap was observed. We present comparative brain/liver glycosylation data on 50 N-glycosylation sites from 34 proteins and 13 O-glycosylation sites from seven proteins. Molecular

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“…Additional examples that are especially relevant to allergic diseases are detailed in an accompanying paper in this volume. 9 …”

Section: Glycans and Glycan Binding Proteins In Immune Regulationmentioning

confidence: 99%

“…Examples relevant to lung inflammatory diseases are discussed in more detail in an accompanying review in this issue. 9 Siglecs function by binding to sialoglycans on their own cell surfaces, on other cells and tissues, and/or on sialic acid-bearing pathogens. 21 The interplay of sialic acids and sialic acid recognition in immune regulation, pathogenesis, and pathogen recognition results in something of an evolutionary arms race as pathogens and hosts respond to changing glycan landscapes.…”

Section: Glycans and Glycan Binding Proteins In Immune Regulationmentioning

confidence: 99%

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Glycans and glycan-binding proteins in immune regulation: A concise introduction to glycobiology for the allergist

Schnaar

2015

Journal of Allergy and Clinical Immunology

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Cells are endowed with a rich surface coat of glycans carried as glycoproteins and glycolipids on the outer leaflet of their plasma membranes and constituting a major molecular interface between cells and their environment. Each cell’s glycome, the sum of its diverse glycan structures, comprises a distinct cellular signature that is defined by the expression levels of the enzymes responsible for glycan biosynthesis. This signature can be read by complementary glycan binding proteins that translate glycan recognition into function. Nowhere is this more evident than in the immune system, where glycans and glycan binding proteins are integral to pathogen recognition and the control of inflammatory responses. Glycobiology – the study of glycan structures and their functions – is increasingly providing insights into immune regulatory mechanisms and thereby providing opportunities for therapeutic intervention. To promote wider appreciation of this rapidly expanding area of research, this review briefly examines the makeup of the human glycome, the glycan binding proteins that translate glycan recognition into function, and provides examples of glycan recognition events that are responsible for immune system regulation.

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Role of siglecs and related glycan-binding proteins in immune responses and immunoregulation

Cited by 97 publications

References 116 publications

The red meat allergy syndrome in Sweden

The red meat allergy syndrome in Sweden

Tissue-Specific Glycosylation at the Glycopeptide Level

Glycans and glycan-binding proteins in immune regulation: A concise introduction to glycobiology for the allergist

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