Human Blood Group ABH/Ii, Lea,b,x,y, and Sialyl Lea,x Glycotopes; Internal Structures; and Immunochemical Roles of Human Ovarian Cyst Glycoproteins

Wu, Albert M.

doi:10.1007/978-1-4419-7877-6_3

Cited by 9 publications

(7 citation statements)

References 40 publications

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“…ABH and l -Fucα1→2 blood group active glycoproteins and the sialic acid-containing glycoproteins were prepared from human ovarian cyst fluid [9] , [10] , [11] , [12] , [13] . The glycan chains of the cyst gps consist of multiple bioactive saccharide branches attached via O -glycosidic linkages at their reducing ends to serine or threonine residues of the polypeptide backbone [11] , [12] .…”

Section: Methodsmentioning

confidence: 99%

Glycan binding profile of a fucolectin-related protein (FRP) encoded by the SP2159 gene of Streptococcus pneumoniae

Singh

Chen

et al. 2018

Biochimie Open

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The recombinant fucolectin-related protein (FRP) of unknown function, encoded by the SP2159 gene of Streptococcus pneumoniae, was expressed in E. coli. In this study, its glycan-recognition epitopes and their binding potencies were examined by enzyme-linked lectinosorbent and inhibition assays. The results indicate that FRP reacted strongly with human blood group ABH and l-Fucα1→2-active glycotopes and in their polyvalent (super) forms. When expressed by mass relative potency, the binding affinities of FRP to poly-l-Fucα1→glycotopes were about 5.0 × 105 folds higher than that of the mono-l-Fucα1→glycotope form. This unique binding property of FRP can be used as a special tool to differentiate complex forms of l-Fucα1→2 and other forms of glycotopes.

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Section: Methodsmentioning

confidence: 99%

Glycan binding profile of a fucolectin-related protein (FRP) encoded by the SP2159 gene of Streptococcus pneumoniae

Singh

Chen

et al. 2018

Biochimie Open

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“…Two Chemical structures of polyvalent l Fucα1→ glycoforms in human blood group A and H active O ‐glycans. (a) asialo porcine salivary glycoproteins (asialo PSM) [14] and (b) human ovarian cyst glycoproteins (cyst gp) [16–19]. Heavy shaded area: potent glycotopes ( l Fucα→2), light shaded area: Ga1β1→3/4GlcNAcβ ( I β / II β ) are weak glycotopes, in which I β / II β are exposed after removal of terminal GalNAcα1→, l Fucα1→ glycotopes as in the cyst P‐1 glycoprotein and Cyst Tighe Phenol P‐1 [18].…”

Section: Methodsmentioning

confidence: 99%

“…ABH and Lewis active blood group active glycoproteins (Cyst Mcdon and Tighe; Structure 1b in Fig. 1) were prepared from human ovarian cyst fluid [16–19]. Human α 1 ‐acid gps and fetuin, which contain multi‐antennary Galβ1→4GlcNAc (II) containing N ‐glycans [20–21], were purchased from Sigma–Aldrich (St Louis, MO, USA).…”

Section: Methodsmentioning

confidence: 99%

Relative intensities of recognition factors at two combining sites of Ralstonia solanacearum lectin (RSL) for accommodating lFucα1→, dManα1→ and Galβ1→3/4GlcNAc glycotopes

Liu

Herp

et al. 2012

FEBS Letters

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Owing to the weak reactivities of monomeric dManα1 and Galβ1→3/4GlcNAcβ (I β/II β) glycotopes with Ralstonia solanacearum lectin (RSL), their recognition roles were previously ignored. In this study, the interaction intensities of RSL toward four monomeric glycotopes lFucα1→, dManα1→ and I β/II β within two combining sites were established by both enzyme‐linked lectinosorbent and inhibition assays. It was found that high density of lFucα1→ complex enhanced the recognition intensities at lFucα1→ site, polyvalent dManα1→ was essential for binding at the dManα1→ site and polyvalent I β/II β was required at lFucα1→ site. The peculiar recognition systems of RSL are very different from other well known microbial lectins.

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“…Human Cyst O-glycoproteins (HOC) -Human blood group ABH active cyst gps (HOC), such as Cyst MSS, Mcdon, Beach, and Tighe etc, were prepared from human ovarian cyst uid and their structures and recognition properties have been investigated for over 70 years [56][57][58][59][60].…”

Section: Polysaccharides-mentioning

confidence: 99%

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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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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Human Blood Group ABH/Ii, Lea,b,x,y, and Sialyl Lea,x Glycotopes; Internal Structures; and Immunochemical Roles of Human Ovarian Cyst Glycoproteins

Cited by 9 publications

References 40 publications

Glycan binding profile of a fucolectin-related protein (FRP) encoded by the SP2159 gene of Streptococcus pneumoniae

Glycan binding profile of a fucolectin-related protein (FRP) encoded by the SP2159 gene of Streptococcus pneumoniae

Relative intensities of recognition factors at two combining sites of Ralstonia solanacearum lectin (RSL) for accommodating lFucα1→, dManα1→ and Galβ1→3/4GlcNAc glycotopes

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

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