Sialic Acid Specificity of Myelin-associated Glycoprotein Binding

Collins, Brian E.; Yang, Lynda J.‐S.; Mukhopadhyay, Gauranga; Filbin, Marie T.; Kiso, Makoto; Hasegawa, Akira; Schnaar, Ronald L.

doi:10.1074/jbc.272.2.1248

Cited by 165 publications

(111 citation statements)

References 62 publications

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“…The ganglioside GD1␣ (and GQ1b␣) contains the same terminal sequence as di-sialyl-T antigen (18) and has been reported to bind to MAG as a high affinity ligand (30). Yet the free oligosaccharide of GD1␣ was found to be only 3-fold more potent an inhibitor of MAG than ␣2-3sialyllactose (4) (26), whereas the disialyl T-antigen was a 1500-fold more potent inhibitor than ␣2-3 sialyllactose in this study.…”

Section: Potent Inhibition Of Mag (Siglec-4) By O-linked Sialosides-tomentioning

confidence: 46%

“…As shown here, the preferential affinity of mCD22 for NeuGc reflects a 10 -20-fold higher affinity for sialosides containing NeuGc over the same sequences containing NeuAc (12 and 13 compared with 19 and 20). Conversely, murine sialoadhesin and murine MAG have been demonstrated to exhibit negligible binding to NeuGc containing oligosaccharides in various multivalent assay systems (27,30,32,39). This preference for NeuAc is reflected in the increased affinity of these siglecs for NeuAc over NeuGc by 2-and 3-8-fold, respectively (Table II).…”

Section: Potent Inhibition Of Mag (Siglec-4) By O-linked Sialosides-tomentioning

confidence: 99%

“…Several reports (25,26,28,39,40) have evaluated the specificity of one or several siglecs using competitive inhibition of multivalent binding assays by monovalent sialosides analogous to the studies reported here. However, most have used multivalent assays based on binding of siglecs to sialosides attached to a polyacrylamide or other polymeric carrier (1,34,37,49,(52)(53)(54)(55)(57)(58)(59), to gangliosides adsorbed to microtiter plates (30,36,38) or to neo-glycoprotein conjugates (27,28).…”

Section: Figmentioning

confidence: 99%

“…No other siglec exhibited a preference for these ␣2-6 sialosides. The preference of sialoadhesin (mSiglec-1) and MAG (mSiglec-4) for the NeuAc␣(2-3)Gal sequence over the NeuAc␣(2-6)Gal sequence (26,27,30,32,34,36) is consistent with the 2-3-and 5-7-fold increased affinity, respectively, for sialosides with the ␣2-3 linkage (4 and 5) over those with the ␣2-6 linkage (12 and 13), in good agreement with results obtained by Strenge et al (26). A preference of Siglecs-9 and -10 for sialosides with the ␣2-3 linkages seen here (1.5-2-fold) was not recognized previously using multivalent probes (51,53,59,61).…”

Section: Potent Inhibition Of Mag (Siglec-4) By O-linked Sialosides-tomentioning

confidence: 99%

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Sialoside Specificity of the Siglec Family Assessed Using Novel Multivalent Probes

Blixt¹,

Collins²,

Nieuwenhof³

et al. 2003

Journal of Biological Chemistry

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206

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Ten of the 11 known human siglecs or their murine orthologs have been evaluated for their specificity for over 25 synthetic sialosides representing most of the major sequences terminating carbohydrate groups of glycoproteins and glycolipids. Analysis has been performed using a novel multivalent platform comprising biotinylated sialosides bound to a streptavidin-alkaline phosphatase conjugate. Each siglec was found to have a unique specificity for binding 16 different sialoside-streptavidin-alkaline phosphatase probes. The relative affinities of monovalent sialosides were assessed for each siglec in competitive inhibition studies. The quantitative data obtained allows a detailed analysis of each siglec for the relative importance of sialic acid and the penultimate oligosaccharide sequence on binding affinity and specificity. Most remarkable was the finding that myelin-associated glycoprotein (Siglec-4) binds with 500 -10,000-fold higher affinity to a series of mono-and di-sialylated derivatives of the O-linked T-antigen (Gal␤(1-3)-GalNAc␣OThr) as compared with ␣-methyl-NeuAc.

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Section: Potent Inhibition Of Mag (Siglec-4) By O-linked Sialosides-tomentioning

confidence: 46%

Section: Potent Inhibition Of Mag (Siglec-4) By O-linked Sialosides-tomentioning

confidence: 99%

Section: Figmentioning

confidence: 99%

Section: Potent Inhibition Of Mag (Siglec-4) By O-linked Sialosides-tomentioning

confidence: 99%

See 2 more Smart Citations

Sialoside Specificity of the Siglec Family Assessed Using Novel Multivalent Probes

Blixt¹,

Collins²,

Nieuwenhof³

et al. 2003

Journal of Biological Chemistry

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206

111

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“…MAG is a sialic-acid-binding lectin (Siglec-4) with high specificity for N-acetylneuraminic acid (Neu5Ac) (Collins et al, 1997). Neu5Ac is the substrate for another prevalent sialic acid, Nglycolylneuraminic acid (Neu5Gc).…”

Section: Modeling the Cause Of The Primary Lesionmentioning

confidence: 99%

The common marmoset (<i>Callithrix jacchus</i>): a relevant preclinical model of human (auto)immune-mediated inflammatory disease of the brain

et al. 2016

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Abstract. The increasing prevalence of chronic autoimmune-mediated inflammatory disorders (AIMIDs) in aging human populations creates a high unmet need for safe and effective medications. However, thus far the translation of pathogenic concepts developed in animal models into effective treatments for the patient has been notoriously difficult. The main reason is that currently used mouse-based animal models for the pipeline selection of promising new treatments were insufficiently predictive for clinical success. Regarding the high immunological similarity between human and non-human primates (NHPs), AIMID models in NHPs can help to bridge the translational gap between rodent and man. Here we will review the preclinical relevance of the experimental autoimmune encephalomyelitis (EAE) model in common marmosets (Callithrix jacchus), a small-bodied neotropical primate. EAE is a generic AIMID model projected on the human autoimmune neuro-inflammatory disease multiple sclerosis (MS).

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A structural difference between the cell surfaces of humans and the great apes

Muchmore

Díaz

Varki

1998

Am. J. Phys. Anthropol.

155

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The sialic acids are major components of the cell surfaces of animals of the deuterostome lineage. Earlier studies suggested that humans may not express N-glycolyl-neuraminic acid (Neu5Gc), a hydroxylated form of the common sialic acid N-acetyl-neuraminic acid (Neu5Ac). We find that while Neu5Gc is essentially undetectable on human plasma proteins and erythrocytes, it is a major component in all the four extant great apes (chimpanzee, bonobo, gorilla and orangutan) as well as in many other mammals. This marked difference is also seen amongst cultured lymphoblastoid cells from humans and great apes, as well as in a variety of other tissues compared between humans and chimpanzees, including the cerebral cortex and the cerebrospinal fluid. Biosynthetically, Neu5Gc arises from the action of a hydroxylase that converts the nucleotide donor CMP-Neu5Ac to CMP-Neu5Gc. This enzymatic activity is present in chimpanzee cells, but not in human cells. However, traces of Neu5Gc occur in some human tissues, and others have reported expression of Neu5Gc in human cancers and fetal tissues. Thus, the enzymatic capacity to express Neu5Gc appears to have been suppressed sometime after the great ape-hominid divergence. As terminal structures on cell surfaces, sialic acids are involved in intercellular cross-talk involving specific vertebrate lectins, as well as in microbe-host recognition involving a wide variety of pathogens. The level of sialic acid hydroxylation (level of Neu5Ac versus Neu5Gc) is known to positively or negatively affect several of these endogenous and exogenous interactions. Thus, there are potential functional consequences of this widespread structural change in humans affecting the surfaces of cells throughout the body.

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Sialic Acid Specificity of Myelin-associated Glycoprotein Binding

Cited by 165 publications

References 62 publications

Sialoside Specificity of the Siglec Family Assessed Using Novel Multivalent Probes

Sialoside Specificity of the Siglec Family Assessed Using Novel Multivalent Probes

The common marmoset (<i>Callithrix jacchus</i>): a relevant preclinical model of human (auto)immune-mediated inflammatory disease of the brain

A structural difference between the cell surfaces of humans and the great apes

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Sialic Acid Specificity of Myelin-associated Glycoprotein Binding

Cited by 165 publications

References 62 publications

Sialoside Specificity of the Siglec Family Assessed Using Novel Multivalent Probes

Sialoside Specificity of the Siglec Family Assessed Using Novel Multivalent Probes

The common marmoset (&lt;i&gt;Callithrix jacchus&lt;/i&gt;): a relevant preclinical model of human (auto)immune-mediated inflammatory disease of the brain

A structural difference between the cell surfaces of humans and the great apes

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Product

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The common marmoset (<i>Callithrix jacchus</i>): a relevant preclinical model of human (auto)immune-mediated inflammatory disease of the brain