Specificity analysis of lectins and antibodies using remodeled glycoproteins

Iskratsch, Thomas; Braun, Andreas; Paschinger, Katharina; Wilson, Iain B. H.

doi:10.1016/j.ab.2008.12.005

Cited by 117 publications

(92 citation statements)

References 83 publications

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“…Each of the lectins tested was however observed to interact with the glycoproteins in an expected fashion based on the glycan structures known to be present on these glycoproteins. For example, the sialic acid binding lectins showed high signals on Fetuin (38) and Thyroglobulin (39), but did not interact with Invertase (40). Conversely, terminal mannose binding lectins interacted strongly with Invertase, but not with Fetuin.…”

Section: Investigation Of Synthetic Blocking Reagentsmentioning

confidence: 99%

Optimization of the enzyme-linked lectin assay for enhanced glycoprotein and glycoconjugate analysis

Thompson

Creavin

O’Connell

et al. 2011

Analytical Biochemistry

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Lectin's are proteins capable of recognising and binding to specific oligosaccharide structures found on glycoproteins and other biomoloecules. As such they have found utility for glycoanalytical applications. One common difficulty encountered in the application of these proteins, particularly in multi-well plate assay formats known as Enzyme Linked Lectin Assays (ELLA's), is in finding appropriate blocking solutions to prevent non-specific binding with plate surfaces. Many commonly used blocking agents contain carbohydrates and generate significant background signals in ELLA's, limiting the utility of the assay.In this study we examined the suitability of a range of blocking reagents, including protein based, synthetic and commercially available carbohydrate free blocking reagents, for ELLA applications. Each blocking reagent was assessed against a panel of 19 commercially available biotinylated lectins exhibiting diverse structures and carbohydrate specificities. We identified the synthetic polymer Polyvinyl Alcohol (PVA) as the best global blocking agent for performing ELLA's. We ultimately present an ELLA methodology facilitating broad spectrum lectin analysis of glycoconjugates and extending the utility of the ELLA.

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Section: Investigation Of Synthetic Blocking Reagentsmentioning

confidence: 99%

Optimization of the enzyme-linked lectin assay for enhanced glycoprotein and glycoconjugate analysis

Thompson

Creavin

O’Connell

et al. 2011

Analytical Biochemistry

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“…Core ␣1,6-fucosylation, a universal animal modification present on many N-glycans of both sources, probably accounts for the lentil lectin (LCA) reactivity (28,29). A novel modification of the core of hemocyte glycans was also observed and is predicted to be the direct modification of the reducing terminal GlcNAc with a hexose as shown by the fragment of m/z 462.…”

Section: N-glycosylation Of Oyster Hemocytes and Plasma-usingmentioning

confidence: 99%

“…of plasma glycans, containing three structures (A), was treated first with bovine ␤-galactosidase (B), followed by jack bean ␤-hexosaminidase (C), chicken ␣-hexosaminidase (D), Xanthomonas ␣1,2-fucosidase (E), and finally ␤1,3-specific galactosidase (F). The progress of digestion of the major structure in this fraction is shown using cans could also account for the reactivity toward Vicia lectin (VVA), which has been previously shown to bind N-acetylgalactosamine-capped N-glycans, O-glycans, and blood group A structures (29,32). The data overall show that oyster glycans are capped in part with a frequently methylated form of the A-type histo-blood group.…”

Section: N-glycosylation Of Oyster Hemocytes and Plasma-usingmentioning

confidence: 99%

Hemocytes and Plasma of the Eastern Oyster (Crassostrea virginica) Display a Diverse Repertoire of Sulfated and Blood Group A-modified N-Glycans*

Kurz

Jin

Hykollari

et al. 2013

Journal of Biological Chemistry

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Background:The eastern oyster, an important estuarine species, is parasitized by a protozoan in a galectin-dependent manner. Results: A variety of paucimannosidic, hybrid, and complex neutral and acidic N-linked oligosaccharides was found. Conclusion:The oyster possesses a complex repertoire of glycans with some features reminiscent of vertebrates. Significance: The N-glycome of the eastern oyster correlates well with the specificity of its own galectin CvGal1.

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“…Crustaceans possess an open circulatory system, where nutrients, oxygen, hormones, and cells are distributed in the hemolymph [1] . Crustaceans lack adaptive immune system and they rely exclusively on their innate immune mechanisms that include both cellular and humoral responses [2] .…”

Section: Introductionmentioning

confidence: 99%