Neuraminic Acid Derivatives Newly Discovered in Humans: N-Acetyl-9-O-L-lactoylneuraminic Acid, N,9-O-Diacetylneuraminic Acid and N-Acetyl-2,3-dehydro-2-deoxyneuraminic Acid

Vliegenthart, J.F.G.; Haverkamp, Johan; Schauer, Roland; Wember, Margret; Farriaux, J. P.; Kamerling, Johannis P.; Versluis, Cees

doi:10.1515/bchm2.1976.357.2.1699

Cited by 66 publications

(18 citation statements)

References 10 publications

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“…1): BSM [22], rat serum [14], human saliva [31], and bovine brain gangliosides [32], all known to contain naturally 9-0-acetylated sialic acids, served as receptors for influenza C virus, whereas glycoconjugates containing other, not 9-0-acetylated sialic acids, like human a,-acid glycoprotein (NeuSAc), GM3 from horse erythrocytes (NeuSGc), and serum glycoproteins from guinea pig with about 35% of its sialic acids as Neu4,5Ac2 [33] did not show receptor activity. Similarly, the neutral glycosphingolipids Lac-Cer and CgOse4-Cer are inactive.…”

Section: Resultsmentioning

confidence: 99%

Use of influenza C virus for detection of 9‐O‐acetylated sialic acids on immobilized glycoconjugates by esterase activity

Zimmer¹,

Reuter²,

Schauer³

1992

European Journal of Biochemistry

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An overlay and a solid-phase assay are presented which allow the specific detection of 9-0-acetylated sialic acids on sialoglycoconjugates immobilized on microtiter plates, nitrocellulose or separated on thin-layer chromatograms. The assay takes advantage of two different biological properties of influenza C virus, its high-affinity binding to 9-0-acetylated sialic acids and its sialate 9-0-acetylesterase that is used for detection of bound virus with fluorogenic or chromogenic substrates. Though simple and rapid, the assay is highly sensitive with a detection limit of 65 fmol9-0-acetylated sialic acid in 9-0-acetylated ganglioside GDla.Influenza C virus is able to bind to a wide spectrum of sialoglycoconjugates like mucins, serum glycoproteins or gangliosides containing naturally or synthetically 0-acetylated sialic acids. 9-0-Acetyl-N-glycoloylneuraminic acid can also function as a high-affinity receptor determinant for influenza C virus. While the acetyl ester at the 9 position is essential for virus binding in all cases, a 4-0-acetyl group is not recognized. In addition to a(2,3) or a(2,6) bonds, 9-0-acetyl-N-acetylneuraminic acid in a(2,8) linkage to N-acetylneuraminic acid is also functionally active.Sialic acids are a Family of about 30 related sugars derived from neuraminic acid, which is the most diversely substituted sugar known in nature. This diversity mainly arises from acetylations that can take place at positions 4,7. 8, and/or 9. In most cases sialic acids occupy the terminal positions of glycoconjugates. Thcir involvement in many biological phenomena, especially as regulation of molecular and cellular recognition is concerned, has been well established [l]. In recent years, the interest in 0-acetylated sialic acids has rapidly increased, since some biological properties of these sugars seem to be associated with these modifications. Examples are the partial or complete block of sialidase action [2,3], binding of influenza C viruses and coronaviruses to cells [4, 51, antigenicity of bacterial capsules [6], modulation of the alternative pathway of complement activation [7], the expression of Nacetyl-9-O-acetylneuraminic acid (Neu5,9Ac2) [8] as a differentiation marker on chicken erythrocytes [9], the association of 9-0-acetylated gangliosides with cell migration in rat brain development [lo], and the expression of an 0-acetylated Correspondence to R. Schauer, Biochemisches Institut, ChristianAlbrechts-Universitat, Okhausenslrasse 40, W-2300 Kiel, Federal Republic of Germany Abbreviution?. RSM, bovine submandibular gland mucin; DMB, 1,2-diamino-4,5-methylenedioxybenzene; ESM, equine submandibular gland mucin; GalNAc, N-acetylgalactosamine; Lac-Cer, lactosylceramide; McUmbAc, 4-methylumbelliferyl acetatc; Neu4,5Ac2, Nacetyl-4-O-acetylneuraminic acid; Neu4AcSGc. N-glycoloyl-4-O-acetylneuraminic acid; Neu5Ac, N-acctylneuraminic acid; Neu5,7Ac2, N-acetyl-7-0-acetylneuraminic acid; Neu5,9Ac2, N-acetyl-9-Oacetylneuraminic acid; NeuSAcgLt, N-acetyl-9-0-lactoylneuraminic acid; Neu9AcSGc, N-glycoloyl-9-0-ac...

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Section: Resultsmentioning

confidence: 99%

Use of influenza C virus for detection of 9‐O‐acetylated sialic acids on immobilized glycoconjugates by esterase activity

Zimmer¹,

Reuter²,

Schauer³

1992

European Journal of Biochemistry

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“…It is known that the major sialic acid in man is Neu5Ac. 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).…”

Section: Discussionmentioning

confidence: 99%

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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“…The earlier reported mass spectrometric characteristics which define the methyl ester, per-0-SiMe, ether derivative of Neu2enSAc [4,5,211 were also detected in the mass spectra of compounds 1 and 3, and in the spectrum of the Me3% ester, per-0-SiMe, ether derivative of Neu2en5Ac [9]. The spectra are dominated by a fragment ion a, occurring at ni/z 227 for methyl ester derivatives and at m/z 285 for Me3Si ester derivatives.…”

Section: Mass Spec Rvometry Ojsynthctic Neuzcnsgc Derivutivesmentioning

confidence: 77%

“…This sialic acid lacks the glycosidic hydroxyl group at C-2. Neu2en5Ac has been found in low concentrations in serum, saliva and urine of healthy individuals [4]. It occurs in much higher concentrations in the serum and urine of a sialuria patient [4,51, wherein the substance was discovered.…”

mentioning

confidence: 99%

“…Neu2en5Ac has been found in low concentrations in serum, saliva and urine of healthy individuals [4]. It occurs in much higher concentrations in the serum and urine of a sialuria patient [4,51, wherein the substance was discovered. Beau et al [6] demonstrated that Neu2enSAc could be obtained from CMP-Neu5Ac at pH values above 7, probably in a non-enzymic elimination reaction.…”

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confidence: 99%

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Structural parameters and natural occurrence of 2-deoxy-2, 3-didehydro-N-glycoloyneuraminic acid

et al. 1985

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2‐Deoxy‐2, 3‐didehydro‐N‐glycoloylneuraminic acid has been found to occur in porcine, bovine and equine submandibular glands as well as in the urine of pig, horse and rat. This novel, unsaturated sialic acid was isolated by gel filtration and ion‐exchange chromatography. Final purification was achieved by column chromatography or by preparative thin‐layer chromatography on cellulose. The structural analysis was performed by combined capillary gas‐liquid chromatography/mass spectrometry. The various data were compared with those from synthetic 2‐deoxy‐2, 3‐didehydro‐N‐acetylated derivative was present in the materials analyzed. The inhibitory effect of 2‐deoxy‐2, 3‐didehydro‐N‐glycoloylneuraminic acid on Vibrio cholerae sialidase using N‐acetylneuraminyl‐(α2→3)‐lactose as substrate is slightly higher (50% inhibition at 10 μM) when compared with 2‐deoxy‐2, 3‐didehydro‐N‐acetylneuraminic acid (50% inhibition at 15 μM).

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Neuraminic Acid Derivatives Newly Discovered in Humans: N-Acetyl-9-O-L-lactoylneuraminic Acid, N,9-O-Diacetylneuraminic Acid and N-Acetyl-2,3-dehydro-2-deoxyneuraminic Acid

Cited by 66 publications

References 10 publications

Use of influenza C virus for detection of 9‐O‐acetylated sialic acids on immobilized glycoconjugates by esterase activity

Use of influenza C virus for detection of 9‐O‐acetylated sialic acids on immobilized glycoconjugates by esterase activity

Attachment of Influenza C Virus to Human Erythrocytes

Structural parameters and natural occurrence of 2-deoxy-2, 3-didehydro-N-glycoloyneuraminic acid

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