Identification of a tetrasialylated monofucosylated tetraantennary <i>N</i>‐linked carbohydrate chain in human platelet glycocalicin

Korrel, Sophia A.M.; Clemetson, Kenneth J.; Halbeek, Herman van; Kamerling, Johannis P.; Sixma, Jan J.; Vliegenthart, Johannes F.G.

doi:10.1016/0014-5793(88)80024-3

Cited by 31 publications

(19 citation statements)

References 17 publications

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“…The carbohydrate structures linked to GPIbα include N- (Korrel et al, 1988) and numerous O-linked carbohydrates throughout the membrane-proximal mucin-like core (Korrel et al, 1984). The N-linked carbohydrates are large, complex, tetraantennary compounds, with terminal branches that consist of NeuAcα ( As expected, GST alone did not bind any of the synthesized carbohydrates (Fig.…”

Section: The Brs Of Gspb and Hsa Bind Different Subsets Of Sialylatedsupporting

confidence: 60%

“…The carbohydrate structures linked to GPIbα include N ‐linked carbohydrates within the N‐terminal globular domain (Korrel et al ., 1988) and numerous O ‐linked carbohydrates throughout the membrane‐proximal mucin‐like core (Korrel et al ., 1984). The N ‐linked carbohydrates are large, complex, tetraantennary compounds, with terminal branches that consist of NeuAcα(2‐3)Galβ(1‐4)GlcNAc [α(2‐3) sialyllactosamine] or NeuAcα(2‐6)Galβ(1‐4)GlcNAc [α(2‐6) sialyllactosamine].…”

Section: Resultsmentioning

confidence: 99%

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Binding of the Streptococcus gordonii surface glycoproteins GspB and Hsa to specific carbohydrate structures on platelet membrane glycoprotein Ibα

Takamatsu¹,

Bensing²,

Cheng

et al. 2005

Molecular Microbiology

125

181

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SummaryGspB and Hsa are homologous serine-rich surface glycoproteins of Streptococcus gordonii strains M99 and Challis, respectively, that mediate the binding of these organisms to platelet membrane glycoprotein (GP) Ib α α α α . Both GspB and Hsa consist of an N-terminal putative signal peptide, a short serine-rich region, a region (BR) that is rich in basic amino acids, a longer serine-rich region and a C-terminal cell wall anchoring domain. To further assess the mechanisms for GspB and Hsa binding, we investigated the binding of the BRs of GspB and Hsa (expressed as glutathione Stranferase fusion proteins) to sialylated glycoproteins in vitro . Both fusion proteins showed significant levels of binding to sialylated moieties on fetuin and GPIb α α α α . In contrast, the corresponding region of a GspB homologue of Streptococcus agalactiae , which is acidic rather than basic, showed no binding to either fetuin or GPIb α α α α . As measured by surface plasmon resonance kinetic analysis, GspB-and Hsaderived fusion proteins had high affinity for GPIb α α α α , but with somewhat different dissociation constants. Dot blot analysis using a panel of synthesized oligosaccharides revealed that the BR of Hsa can bind both α α α α (2-3) sialyllactosamine [NeuAc α α α α (2-3)Gal β β β β (1-4)GlcNAc] and sialyl-T antigen [NeuAc α α α α (2-3)Gal β β β β (1-3)GalNAc], whereas the BR of GspB only bound sialyl-T antigen. Moreover, far Western blotting using platelet membrane proteins revealed that GPIb α α α α is the principal receptor for GspB and Hsa on human platelets. The combined results indicate that the BRs of GspB and Hsa are the binding domains of these adhesins. However, the subsets of carbohydrate structures on GPIb α α α α recognized by the binding domains appear to be different between the two proteins.

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Section: The Brs Of Gspb and Hsa Bind Different Subsets Of Sialylatedsupporting

confidence: 60%

Section: Resultsmentioning

confidence: 99%

Binding of the Streptococcus gordonii surface glycoproteins GspB and Hsa to specific carbohydrate structures on platelet membrane glycoprotein Ibα

Takamatsu¹,

Bensing²,

Cheng

et al. 2005

Molecular Microbiology

125

181

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“…Previous studies of the platelet glycoprotein GPIbα identified a core 2 hexasaccharide comprised of sialyl-T antigen with β1–6 glycosidic linkage between the GlcNAc in 3'-sialyllactosamine Siaα2–3Galβ1–4GlcNAc and the core GalNAc in the sialyl-T antigen 42, 43 (this structure is shown in the conceptual model in Fig. 11B).…”

Section: Discussionmentioning

confidence: 89%

Structures of the Streptococcus sanguinis SrpA Binding Region with Human Sialoglycans Suggest Features of the Physiological Ligand

Loukachevitch

Bensing

et al. 2016

Biochemistry

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Streptococcus sanguinis is a leading cause of bacterial infective endocarditis, a life threatening infection of heart valves. S. sanguinis binds to human platelets with high avidity, and this adherence is likely to enhance virulence. Previous studies suggest that a serine-rich repeat adhesin termed SrpA mediates the binding of S. sanguinis to human platelets via its interaction with sialoglycans on the receptor GPIbα. However, in vitro binding assays between SrpA and defined sialoglycans failed to identify specific high-affinity ligands. To better understand the interaction between SrpA and human platelets, we determined cocrystal structures of the SrpA sialoglycan binding region (SrpABR) with five low-affinity ligands: three sialylated trisaccharides (sialyl-T antigen, 3'-sialyllactose, and 3'-sialyl-N-acetyllactosamine), a sialylated tetrasaccharide (sialyl-LewisX) and a sialyl galactose disaccharide component common to these sialoglyans. We then combined structural analysis with mutagenesis to further determine whether our observed interactions between SrpABR and glycans are important for binding to platelets and to better map the binding site for the physiological receptor. We found that the sialoglycan binding site of SrpABR is significantly larger than the sialoglycans cocrystallized in this study, which suggests that SrpA binding to platelets is either multivalent or occurs via a larger, disialylated glycan.

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“…The GPIb␣ N-terminal domain contains the di-, tri-, and tetra-antennary N-linked glycans, 44,45 whereas O-linked glycans reside within the C-terminal domain. 46,47 It is probable that in vivo and in vitro removal of platelets occurs via exposed ␤Gal residues on N-linked glycans rather than on O-linked glycans, consistent with the shown effects of ligand valency (tetra-, Ͼ tri-, Ͼ di-, Ͼ mono-antennary) and sugar spacing (20 Å Ͼ 10 Å Ͼ 4 Å) on glycan binding to ASGPRs.…”

Section: Discussionmentioning

confidence: 99%

Role of sialic acid for platelet life span: exposure of β-galactose results in the rapid clearance of platelets from the circulation by asialoglycoprotein receptor–expressing liver macrophages and hepatocytes

Sørensen

Rumjantseva

Nayeb-Hashemi

et al. 2009

Blood

201

180

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Although surface sialic acid is considered a key determinant for the survival of circulating blood cells and glycoproteins, its role in platelet circulation lifetime is not fully clarified. We show that thrombocytopenia in mice deficient in the St3gal4 sialyltransferase gene (St3Gal-IV ؊/؊ mice) is caused by the recognition of terminal galactose residues exposed on the platelet surface in the absence of sialylation. This results in accelerated platelet clearance by asialoglycoprotein receptorexpressing scavenger cells, a mechanism that was recently shown to induce thrombocytopenia during Streptococcus pneumoniae sepsis. We now identify platelet GPIb␣ as a major counterreceptor on ST3Gal-IV ؊/؊ platelets for asialoglycoprotein receptors. Moreover, we report data that establish the importance of sialylation of the von Willebrand factor in its function. (Blood. 2009;114:1645-1654)

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Identification of a tetrasialylated monofucosylated tetraantennary N‐linked carbohydrate chain in human platelet glycocalicin

Cited by 31 publications

References 17 publications

Binding of the Streptococcus gordonii surface glycoproteins GspB and Hsa to specific carbohydrate structures on platelet membrane glycoprotein Ibα

Binding of the Streptococcus gordonii surface glycoproteins GspB and Hsa to specific carbohydrate structures on platelet membrane glycoprotein Ibα

Structures of the Streptococcus sanguinis SrpA Binding Region with Human Sialoglycans Suggest Features of the Physiological Ligand

Role of sialic acid for platelet life span: exposure of β-galactose results in the rapid clearance of platelets from the circulation by asialoglycoprotein receptor–expressing liver macrophages and hepatocytes

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