Recognition Roles of Mammalian Structural Units and Polyvalency in Lectin–Glycan Interactions

Wu, Albert M.; Liu, Jia-Haw; Singh, T. N.; Yang, Zhangung

doi:10.1007/978-1-4419-7877-6_6

Cited by 7 publications

(7 citation statements)

References 62 publications

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“…The glycan codes for Gal/GalNAc speci c lectin-glycan interactions has been de ned since early 1990 [7,31]. It is one of the best and easy ways to elucidate the structures and functional roles of Gal/GalNAc related glycan complexes.…”

Section: Discussionmentioning

confidence: 99%

“…The Factors involved in the recognition process of the lectin-glycan interactions are de ned as Recognition Factors (RFs) [31]. During the past 70 years, six of them have been selected and applied to demonstrate the mammalian Gal/GalNAc related glycoconjugate-glycan interactions [7,31,35,60]. They are: (i) Sub-monosaccharide speci city: anomers and epimers in the pyranose form of monosaccharides;…”

Section: Expressions Of the Intensities And Avidities Of Recognition ...mentioning

confidence: 99%

“…Although RFs of the most (ii)-(iv) [i.e RF-2 to RF-5] are the weak ones, while they are the essential and core elements in the recognition process, which are similar to amino acids peptide sequence in a protein. They have also been used to classify the applied lectins [7,31,35]. As the intensities and avidities of the polyvalency of the Gal/GalNAc related glycotopes and their resulting conformational features [RF-(vi)] has been found to be the critical factor for the most mechanism of lectin-glycan interactions.…”

Section: Expressions Of the Intensities And Avidities Of Recognition ...mentioning

confidence: 99%

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Roles of the structural units, glycotopes / mammalian N-glycans for Con A - Glycan interactions, their codes, and their recognition Factors

2023

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The binding property of Con A has been studied intensively and applied widely to glycoconjugates / glycobiology for over 80 years. However, its role and functional relationship of Con A with these mammalian structural units, glycotopes, N-glycan chains, as well as their polyvalent forms in N-glycoproteins involved in the Con A- glycan interactions have not been all defined and organzied. In this study, the recognition factors involved in these inteactions were azalyzed by our well developed method- the enzyme linked lectinosorbent (ELLSA) and inhibition assay. Based on all data obtained, it is concluded that Con A, as previous report, has a relatively broad and wide recognition ability with the Manα1→ and Glcα1→ related glycans. In addition to it reacted strongly with yeast mannan and glycogens, it also bound well with a large number of mammalian N-glycans, including the N-glycans of rat sublingual gp (RSL), human Tamm-Horsfall glycoprotein (THGP), thyroglobin and lactosferrin. The recognition specificity of Con A towards ligands, expressed by Molar Relative Potency (Molar R.P.), in a decreasing order is as follows: a1→3, a1→6 Mannopentaose (M5) and Biantennary N-linked core pentasaccharide (MDi) ≥ a1→3, a1→6 Mannotriose (M3) > Mana1→3Man (α1→3Mannobiose), Mana1→2Man (α1→2Mannobiose), Mana1→6Man (α1→6Mannobiose), Mana1→4Man (α1→4Mannobiose) > GlcNAcb1→2Man (b1→2 N-Acetyl glucosamine-mannose) > Mana1→/Glcα1→ > Man > Glc, while Gal / GalNAc were inactive. Furthermore, the Man related code system, in this study, is proposed to express by both numbers of Man and GlcNAcb1→ branches (M3 to M9 / MMono to Penta etc.) and a table of three Mana1→ and Glca1→ related biomasses of six recognition factors involved in the Con A-glycan interactions has also been demonstrated. These themes should be one of the most valuable advances since 1980s.

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Section: Discussionmentioning

confidence: 99%

Section: Expressions Of the Intensities And Avidities Of Recognition ...mentioning

confidence: 99%

Section: Expressions Of the Intensities And Avidities Of Recognition ...mentioning

confidence: 99%

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Roles of the structural units, glycotopes / mammalian N-glycans for Con A - Glycan interactions, their codes, and their recognition Factors

2023

Preprint

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Section: Discussionmentioning

confidence: 99%

“…Lectins are an important class of proteins or glycoproteins of non-immune origin that bind non-covalently to characteristic carbohydrate structures with speci city or selectivity [1][2][3][4]. They have been widely used as tools to probe the structural and functional roles of cell surface carbohydrates and to fractionate soluble or membrane glycoproteins of diverse origins and de ned as applied lectins [1][2][3][4][5][6][7]. Based on lectin-reactive monosaccharides with the highest a nity, the applied lectins have been divided in ve speci city groups [1,5,6].…”

Section: Introductionmentioning

confidence: 99%

Roles of the structural units, glycotopes / mammalian N-glycans for Con A-glycan interactions, their codes, and their recognition factors

2023

Glycoconj J

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The binding property of Con A has been studied intensively and applied widely to glycoconjugates / glycobiology for over 80 years. However, its role and functional relationship of Con A with these mammalian structural units, glycotopes, N-glycan chains, as well as their polyvalent forms in Nglycoproteins involved in the Con A-glycan interactions have not been all de ned and organzied. In this study, the recognition factors involved in these inteactions were azalyzed by our well developed methodthe enzyme linked lectinosorbent (ELLSA) and inhibition assay. Based on all data obtained, it is concluded that Con A, as previous report, has a relatively broad and wide recognition ability with the Manα1→ and Glcα1→ related glycans. In addition to it reacted strongly with yeast mannan and glycogens, it also bound well with a large number of mammalian N-glycans, including the N-glycans of rat sublingual gp (RSL), human Tamm-Horsfall glycoprotein (THGP), thyroglobin and lactosferrin. The recognition speci city of Con A towards ligands, expressed by Molar Relative Potency (Molar R.P.), in a decreasing order is as follows: a1→3, a1→6 Mannopentaose (M 5 ) and Biantennary N-linked core pentasaccharide (M Di ) ≥ a1→3, a1→6 Mannotriose (M 3 ) > Mana1→3Man (α1→3Mannobiose), Mana1→2Man (α1→2Mannobiose), Mana1→6Man (α1→6Mannobiose), Mana1→4Man (α1→4Mannobiose) > GlcNAcb1→2Man (b1→2 N-Acetyl glucosamine-mannose) > Mana1→/Glcα1→ > Man > Glc, while Gal / GalNAc were inactive. Furthermore, the Man related code system, in this study, is proposed to express by both numbers of Man and GlcNAcb1→ branches (M 3 to M 9 / M Mono to Penta etc. ) and a table of three Mana1→ and Glca1→ related biomasses of six recognition factors involved in the Con A-glycan interactions has also been demonstrated. These themes should be one of the most valuable advances since 1980s.

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Stationary phases for the enrichment of glycoproteins and glycopeptides

et al. 2014

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The analysis of protein glycosylation is important for biomedical and biopharmaceutical research. Recent advances in LC-MS analysis have enabled the identification of glycosylation sites, the characterisation of glycan structures and the identification and quantification of glycoproteins and glycopeptides. However, this type of analysis remains challenging due to the low abundance of glycopeptides in complex protein digests, the microheterogeneity at glycosylation sites, ion suppression effects and the competition for ionisation by co-eluting peptides. Specific sample preparation is necessary for comprehensive and site-specific glycosylation analyses using MS. Therefore, researchers continue to pursue new columns to broaden their applications. The current manuscript covers recent literature published from 2008 to 2013. The stationary phases containing various chemical bonding methods or ligands immobilisation strategies on solid supports that selectively enrich N-linked or sialylated N-glycopeptides are categorised with either physical or chemical modes of binding. These categories include lectin affinity, hydrophilic interactions, boronate affinity, titanium dioxide affinity, hydrazide chemistry and other separation techniques. This review should aid in better understanding the syntheses and physicochemical properties of each type of stationary phases for enriching glycoproteins and glycopeptides.

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Recognition Roles of Mammalian Structural Units and Polyvalency in Lectin–Glycan Interactions

Cited by 7 publications

References 62 publications

Roles of the structural units, glycotopes / mammalian N-glycans for Con A - Glycan interactions, their codes, and their recognition Factors

Roles of the structural units, glycotopes / mammalian N-glycans for Con A - Glycan interactions, their codes, and their recognition Factors

Roles of the structural units, glycotopes / mammalian N-glycans for Con A-glycan interactions, their codes, and their recognition factors

Stationary phases for the enrichment of glycoproteins and glycopeptides

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