Interaction of wheat germ agglutinin with sialic acid

Peters, Barry P.; Ebisu, Shigeyuki; Goldstein, Irwin J.; Flashner, Michael

doi:10.1021/bi00591a038

Cited by 249 publications

(131 citation statements)

References 31 publications

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“…The observation that a minority of HPA-binding HSV oligosaccharides adsorbed to WGA, might indicate the presence of sialic acid or GlcNAc (Goldstein & Hayes, 1978;Peters et al, 1979). However, since our results of sialidase treatment and DEAE-Sephacel chromatography were not consistent with such an assumption, the binding to WGA seems rather to be due to internal/~-linked GIcNAc residues.…”

Section: Discussioncontrasting

confidence: 55%

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Glycoprotein C of Herpes Simplex Virus Type 1: Characterization of O-linked Oligosaccharides

Olofsson

Sjöblom

Lundström

et al. 1983

Journal of General Virology

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SUMMARYIn contrast to other viral glycoproteins, the herpes simplex virus (HSV) glycoprotein C (gC) binds to the N-acetylgalactosamine-specific Helix pomatia lectin (HPA). In the present paper gC was purified by affinity chromatography with monospecific antibodies and the purified glycoprotein was subjected to protease digestion. HPAbinding protease-resistant glycopeptides were isolated by lectin affinity chromatography. The isolated structures did not bind to concanavalin A and seemed to lack charged groups as determined by ion-exchange chromatography. In gel filtration, the glycopeptides appeared in two peaks with molecular weights higher than 4000. The HPA-binding structures of gC were synthesized in the presence of tunicamycin, indicating that they belong to the O-glycosyl class of oligosaccharides. In addition to HPA-binding oligosaccharides, synthesis of tunicamycin-resistant wheat germ lectinbinding gC oligosaccharides was demonstrable. These were sensitive to sialidase and apparently unrelated to the HPA-binding oligosaccharides.

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Section: Discussioncontrasting

confidence: 55%

“…WGA affinity of carbohydrates is mainly due to the presence of fl-linked GlcNAc or sialic acid (Peters et al, 1979;G oldstein & Hayes, 1978). WGA-binding properties of TM-resistant gC oligosaccharides may therefore be attributed to sialic acid linked to and perhaps blocking an HPA-binding penultimate GalNAc.…”

Section: Tm-resistant Wga-binding Oligosaccharidesmentioning

confidence: 99%

Glycoprotein C of Herpes Simplex Virus Type 1: Characterization of O-linked Oligosaccharides

Olofsson

Sjöblom

Lundström

et al. 1983

Journal of General Virology

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“…We noted a slight reduction in the binding of WGA to inhibitortreated cells. This can be explained by the cross-reactivity of lectin to sialic acids rather than by alterations in the expression of GlcNAc (38,39). Noteworthy, even at the highest concentrations used, tumor cell viability was unaffected by the inhibitor (data not shown).…”

Section: P-3f Ax -Neu5ac Selectively Inhibits Sialylation In Murine Mmentioning

confidence: 91%

Targeting Aberrant Sialylation in Cancer Cells Using a Fluorinated Sialic Acid Analog Impairs Adhesion, Migration, and In Vivo Tumor Growth

Büll

Boltje

Wassink

et al. 2013

Molecular Cancer Therapeutics

157

133

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Cancer cells decorate their surface with a dense layer of sialylated glycans by upregulating the expression of sialyltransferases and other glycogenes. Although sialic acids play a vital role in many biologic processes, hypersialylation in particular has been shown to contribute to cancer cell progression and metastasis. Accordingly, selective strategies to interfere with sialic acid synthesis might offer a powerful approach in cancer therapy. In the present study, we assessed the potential of a recently developed fluorinated sialic acid analogue (P-3F ax -Neu5Ac) to block the synthesis of sialoglycans in murine melanoma cells and the consequences on cell adhesion, migration, and in vivo growth. The results showed that P-3F ax -Neu5Ac readily caused depletion of a2,3-/a2,6-linked sialic acids in B16F10 cells for several days. Long-term inhibition of sialylation for 28 days was feasible without affecting cell viability or proliferation. Moreover, P-3F ax -Neu5Ac proved to be a highly potent inhibitor of sialylation even at high concentrations of competing sialyltransferase substrates. P-3F ax -Neu5Ac-treated cancer cells exhibited impaired binding to poly-L-lysine, type I collagen, and fibronectin and diminished migratory capacity. Finally, blocking sialylation of B16F10 tumor cells with this novel sialic acid analogue reduced their growth in vivo. These results indicate that P-3F ax -Neu5Ac is a powerful glycomimetic capable of inhibiting aberrant sialylation that can potentially be used for anticancer therapy. Mol Cancer Ther; 12(10); 1935-46. Ó2013 AACR.

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“…Although WGA is a D-GlcNAc and Neu5Ac specific lectin [25][26][27][28], it did not bind to compounds 1 and 2, both having a terminal Neu5Ac residue, and to compound 3 with a terminal Neu5Ac and a terminal GlcNAc residue (table I). It should be noted that the indicated compounds have Neu5Ac (1-3) or GlcNAc (3) in a branched rather than in a linear situation.…”

Section: Binding Properties Of Oligosaccharides 1-5 With Different Lementioning

confidence: 99%

Analysis of the interaction between lectins and tetra- and tri-saccharide mimics of the Sda determinant by surface plasmon resonance detection

et al. 2001

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Interaction of wheat germ agglutinin with sialic acid

Cited by 249 publications

References 31 publications

Glycoprotein C of Herpes Simplex Virus Type 1: Characterization of O-linked Oligosaccharides

Glycoprotein C of Herpes Simplex Virus Type 1: Characterization of O-linked Oligosaccharides

Targeting Aberrant Sialylation in Cancer Cells Using a Fluorinated Sialic Acid Analog Impairs Adhesion, Migration, and In Vivo Tumor Growth

Analysis of the interaction between lectins and tetra- and tri-saccharide mimics of the Sda determinant by surface plasmon resonance detection

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