The challenges of glycan recognition with natural and artificial receptors

Tommasone, Stefano; Allabush, Francia; Tagger, Yazmin K.; Norman, Joshua; Köpf, Monika; Tucker, James H. R.; Mendes, Paula M.

doi:10.1039/c8cs00768c

Cited by 126 publications

(119 citation statements)

References 163 publications

(186 reference statements)

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“…Recombinant lectins can also be used to label glycans present on the membrane of intact cells for detection by flow cytometry or microscopy (Bull et al, 2015), but their multimeric nature and relatively weak binding strength (Debray et al, 1981) may complicate data interpretation. Antibodies against glycan antigens are limited due to glycan low immunogenicity and high structural similarity (Tommasone et al, 2019). Another way to label membrane-exposed glycan structures on intact cells or in cell lysates is chemoenzymatic labeling, which exploits engineered recombinant glycosyltranferases that add monosaccharide analogs, suitable for click chemistry reactions, to specific structures in glycan chains (Lopez Aguilar et al, 2017).…”

Section: Quantitative and Qualitative Measurement Of Receptor Glycosymentioning

confidence: 99%

Biological and Technical Challenges in Unraveling the Role of N-Glycans in Immune Receptor Regulation

et al. 2020

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N-glycosylation of membrane receptors is important for a wide variety of cellular processes. In the immune system, loss or alteration of receptor glycosylation can affect pathogen recognition, cell-cell interaction, and activation as well as migration. This is not only due to aberrant folding of the receptor, but also to altered lateral mobility or aggregation capacity. Despite increasing evidence of their biological relevance, glycosylation-dependent mechanisms of receptor regulation are hard to dissect at the molecular level. This is due to the intrinsic complexity of the glycosylation process and high diversity of glycan structures combined with the technical limitations of the current experimental tools. It is still challenging to precisely determine the localization and site-occupancy of glycosylation sites, glycan micro-and macro-heterogeneity at the individual receptor level as well as the biological function and specific interactome of receptor glycoforms. In addition, the tools available to manipulate N-glycans of a specific receptor are limited. Significant progress has however been made thanks to innovative approaches such as glycoproteomics, metabolic engineering, or chemoenzymatic labeling. By discussing examples of immune receptors involved in pathogen recognition, migration, antigen presentation, and cell signaling, this Mini Review will focus on the biological importance of N-glycosylation for receptor functions and highlight the technical challenges for examination and manipulation of receptor N-glycans.

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Section: Quantitative and Qualitative Measurement Of Receptor Glycosymentioning

confidence: 99%

Biological and Technical Challenges in Unraveling the Role of N-Glycans in Immune Receptor Regulation

et al. 2020

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“…Carbohydrates—along with lipids, nucleic acids and proteins—are representatives of the biomolecules essential for life with glycans (complex carbohydrates) densely covering the cellular surface with involvement in numerous processes [ 1 , 2 ]. A glycome is a complete collection of all the glycans present in cells, tissues or organisms at any particular time [ 3 ].…”

Section: Glycomicsmentioning

confidence: 99%

“…For example lectins bind to monosaccharides with affinity constant in the millimolar range [ 2 ]. Oligosaccharides bind to lectins with affinity constant in the micromolar range despite the fact that oligosaccharides can bind to lectins via multiple contacts [ 1 ]. This is due to absence of a deeper binding pocket on the surface of lectins allowing competitive solvent interactions [ 1 ].…”

Section: Glycomicsmentioning

confidence: 99%

“…Oligosaccharides bind to lectins with affinity constant in the micromolar range despite the fact that oligosaccharides can bind to lectins via multiple contacts [ 1 ]. This is due to absence of a deeper binding pocket on the surface of lectins allowing competitive solvent interactions [ 1 ]. On the other hand, interaction of lectins with monosaccharides can be enhanced in cases lectins are assembled from homo-oligomeric subunits and each subunit interacts with a monosaccharide [ 1 ].…”

Section: Glycomicsmentioning

confidence: 99%

“…This is due to absence of a deeper binding pocket on the surface of lectins allowing competitive solvent interactions [ 1 ]. On the other hand, interaction of lectins with monosaccharides can be enhanced in cases lectins are assembled from homo-oligomeric subunits and each subunit interacts with a monosaccharide [ 1 ].…”

Section: Glycomicsmentioning

confidence: 99%

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Glycan Nanobiosensors

et al. 2020

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This review paper comprehensively summarizes advances made in the design of glycan nanobiosensors using diverse forms of nanomaterials. In particular, the paper covers the application of gold nanoparticles, quantum dots, magnetic nanoparticles, carbon nanoparticles, hybrid types of nanoparticles, proteins as nanoscaffolds and various nanoscale-based approaches to designing such nanoscale probes. The article covers innovative immobilization strategies for the conjugation of glycans on nanoparticles. Summaries of the detection schemes applied, the analytes detected and the key operational characteristics of such nanobiosensors are provided in the form of tables for each particular type of nanomaterial.

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Targeting Oligosaccharides and Glycoconjugates Using Superselective Binding Scaffolds

Tommasone

Tagger

Mendes

2020

Adv Funct Materials

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Recognition of oligosaccharides is associated with very limited specificity due to their strong solvation in water and the high degree of subtle structural variations between them. Here, oligosaccharide recognition sites are created on material surfaces with unmatched, binary on–off binding behavior, sharply discriminating a target oligosaccharide over closely related carbohydrate structures. The basis for the superselective binding behavior relies on the highly efficient generation of a pure, high order complex of the oligosaccharide target with synthetic carbohydrate receptor sites, in which the spatial arrangement of the multiple receptors in the complex is preserved upon material surface incorporation. The synthetic binding scaffolds can easily be tailored to recognize different oligosaccharides and glycoconjugates, opening up a realm of possibilities for their use in a wide field of applications, ranging from life sciences to diagnostics.

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The challenges of glycan recognition with natural and artificial receptors

Abstract: Development of natural and artificial receptors with high affinity and exquisite specificity for various purposes remains an important goal and challenge.

Cited by 126 publications

References 163 publications

Biological and Technical Challenges in Unraveling the Role of N-Glycans in Immune Receptor Regulation

Biological and Technical Challenges in Unraveling the Role of N-Glycans in Immune Receptor Regulation

Glycan Nanobiosensors

Targeting Oligosaccharides and Glycoconjugates Using Superselective Binding Scaffolds

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