Occurrence of Sialic Acids

Corfield, Anthony P.; Schauer, Roland

doi:10.1007/978-3-7091-8680-0_2

Cited by 130 publications

(43 citation statements)

References 315 publications

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“…OAcetylated sialic acids, particularly Neu5,9Ac2, have also been shown to exist, though in low levels, in brain (Haverkamp et al, 1977), saliva (Haverkamp et al, 1976), colonic mucins (Rogers et al, 1978), B lymphocytes (Kamerling et al, 1982) and several melanoma cell lines (Cheresh et al, 1984). No biochemical evidence has been presented yet, however, for the presence of O-acetylated sialic acids in human erythrocytes (Corfield & Schauer, 1982). Identification of O-acetylated sialic acids on human erythrocyte membranes in this study suggests that the influenza C virus binding assay is much more sensitive in detecting these types of sialic acid than any of the chemical methods previously used.…”

Section: Discussionmentioning

confidence: 57%

“…The recent study of Rogers et al (1986) suggested that the agglutination of vertebrate erythrocytes correlated well with the presence of Neu5,9Ac2 on their surface. The ability of influenza C virus to agglutinate human erythrocytes, however, remains unexplained; although human erythrocytes from some individuals were agglutinated in high titres (Minuse et al, 1954;Chakraverty, 1978;Ohuchi et al, 1978), the presence of O-acetylated sialic acids, including Neu5,9Ac2, has never been detected on the erythrocyte membrane (Corfield & Schauer, 1982).…”

Section: Introductionmentioning

confidence: 99%

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Attachment of Influenza C Virus to Human Erythrocytes

Nishimura

Sugawara²,

Kitame³

et al. 1988

Journal of General Virology

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SUMMARYBinding experiments with radioactively labelled influenza C virions were carried out to investigate the interaction of the virus with human erythrocytes. The erythrocytes from any of 35 different individuals were found to contain influenza C virus-binding sites though their number was variable among the individuals and was much less than that on mouse, rat and chicken erythrocytes. Attachment of influenza C virus to human erythrocytes was inhibited completely by prior treatment of the virus with anti-HE monoclonal antibody having a strong haemagglutination inhibition activity. Pretreatment of erythrocytes with neuraminidase or the neuraminate-O-acetylesterase of influenza C virus resulted in a marked reduction in the level of virus binding. Thus it appears that human erythrocytes have a low level of O-acetylated sialic acid-containing glycoconjugates that can interact specifically with the HE glycoprotein of influenza C virus. Proteolytic digestion of erythrocytes with ficin, bromelain or V-8 protease inhibited virus binding almost completely, suggesting that the erythrocyte receptor for influenza C virus is a glycoprotein. In contrast to these enzymes, trypsin treatment of erythrocytes reduced virus binding by only about 50~, and ~-chymotrypsin treatment did not inhibit at all. It was also found that treatment of erythrocytes with monoclonal antibody to the M or N blood group antigen greatly inhibited virus binding to the cells. These results, taken together, suggest that most influenza C virus receptors on human erythrocytes, if not all, reside on glycophorin A which is known to possess the M or N blood group activity.

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Section: Discussionmentioning

confidence: 57%

Section: Introductionmentioning

confidence: 99%

Attachment of Influenza C Virus to Human Erythrocytes

Nishimura

Sugawara²,

Kitame³

et al. 1988

Journal of General Virology

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“…That both NeuAc-and NeuGc-containing oligosaccharides can occur in the same glycoprotein is of particular interest [35]. In 1985 Sherblom and Dahlin [lo] showed that both species were present in tumour cell glycoproteins and so the proportions of each present in PSM are worth consideration.…”

Section: Discussionmentioning

confidence: 99%

Porcine submaxillary mucin contains α2→3‐ and α2→6‐linked N‐acetyl‐ and N‐glycolyl‐neuraminic acid

Savage

Koppen

Schiphorst

et al. 1986

European Journal of Biochemistry

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Four acidic trisaccharides have been obtained by alkaline borohydride reductive cleavage (8-elimination) of a fraction of porcine submaxillary mucin precipitating at 60 -75% ethanol. Their structures have been investigated using the techniques of methylation analysis involving gas-liquid chromatography/mass spectrometry along with high-resolution 'H-NMR analysis. Two of the four oligosaccharides, B1-B4, contain N-acetylneuraminic acid (NeuAc) while two contain N-glycolylneuraminic acid (NeuGc). The following structures are proposed for the acidic trisaccharide fraction: (Bl) NeuAca(2-+3)Gal~(l-+3)GalNAcol, (B2) NeuGca(2+3)Galj?(1+3)GalNAcol,These oligosaccharides were present in a molar ratio of 69: 22: 4: 5. Although oligosaccharide B4 has previously been found in porcine submaxillary much B1, B2 and B3 have not. Furthermore, oligosaccharide B2 is a novel structure.The oligosaccharide structures of porcine submaxillary mucin and their biosynthesis have been the subject of many investigations [l -91. Some questions have, however, remained unanswered. For instance, Rearick et al. [q have reported the characterization of porcine submaxillary P-galactoside a2 +3-sialyltransferase, to form the sequence NeuAca(2-t 3)-Galfl(1+3)GalNAc, although this structural element had not been reported in porcine submaxillary mucin (PSM). In addition, a study by Sherblom and Dahlin [lo] showing that both NeuAc and NeuGc were present in tumour cell glycoproteins, along with the report of Buscher et al. [l 11 on the biosynthesis of NeuGc in porcine submaxillary glands and the considerable controversy which has surrounded the oligosaccharide structures of PSM [3 -51 prompted a further investigation.The mucin was precipitated from porcine submaxillary gland extracts using a higher alcohol concentration than that employed by earlier investigators. Oligosaccharides were released by P-elimination, and their structures were determined by high-resolution 'H-NMR spectroscopy and methylation analysis. Four sialic-acid-containing trisaccharides, three of Correspondence to A. V. Savage, Department of Chemistry, University College, Galway, IrelandAbbreviations. GalNAcul, reduced N-acetylgalactosamine; NeuAc, N-acetylneuraminic acid; NeuGc, N-glycolylneuraminic acid; HPLC, high-pressure liquid chromatography; GLC-MS, gasliquid chromatography/mass spectrometry; PSM, porcine submaxillary mucin.Enzymes. P-Galactoside ct2-+3-sialyltransferase (EC 2.4.99.4); NeuAc : a-N-acetylgalactosaminide a 2 +6-sialyltransferase (EC 2.4.99.3); N-acetylneuraminate monooxygenase (EC 1.14.99.18). which had not previously been described in PSM and one of which is novel, were found. MATERIALS AND METHODS Isolation of oligosaccharidesMucin was isolated from porcine submaxillary glands according to de Salegui and Plonska [12] except that additional precipitates were obtained: following the removal of the 48 -54% and 54 -60% ethanol precipitates by centrifugation, the mucin solution was brought to 75% (v/v) ethanol, allowed to stand at 4°C for 16 hand centrifuged at 270...

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“…An uneven distribution of sialic acids in N-and 0-linked oligosaccharides is unusual and therefore of particular interest [31]. In the bovine blood coagulation factor X for instance, the N-glycans contain only NeuAc, whereas in the mucin-type structures both NeuAc and NeuGc are present [32].…”

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confidence: 99%

The N‐and O‐linked carbohydrate chains of human, bovine and porcine plasminogen

Marti

Schaller

Rickli

et al. 1988

European Journal of Biochemistry

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The structures of the N‐and O‐glycans of human, bovine and porcine plasminogen were determined by 500‐MHz 1H‐NMR spectroscopy. The N‐glycans of all three species proved to be of the N‐acetyllactosamine type differing from one another with respect to the sialylation and fucosylation patterns. In the N‐glycan of human plasminogen the two antennae are sialylated with N‐acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N‐glycolylneuraminic acid (NeuGc). In porcine plasminogen the sialic acid is mainly NeuAc; the Manα1→6 branch, however, is only partially sialylated. In addition, the porcine N‐glycan is fucosylated to about 80% in α1→6 linkage to the GlcNAc‐1 residue. The O‐glycans of the three species possess an identical Galβ1→3GalNAc core which is α2→3 sialylated with NeuAc at Gal. The disialylated form, which is also present in all three species, has an additional NeuAc residue in α2→6 linkage to GalNAc. Mono‐and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine. This study on the carbohydrate moiety of these three plasminogens reveals species specificity in terms of various types of microheterogeneities.

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Occurrence of Sialic Acids

Cited by 130 publications

References 315 publications

Attachment of Influenza C Virus to Human Erythrocytes

Attachment of Influenza C Virus to Human Erythrocytes

Porcine submaxillary mucin contains α2→3‐ and α2→6‐linked N‐acetyl‐ and N‐glycolyl‐neuraminic acid

The N‐and O‐linked carbohydrate chains of human, bovine and porcine plasminogen

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