Neuraminidase inhibition by chemically sulphated glycopeptides

Mian, Nasi; Anderson, Caroline; Kent, P. W.

doi:10.1042/bj1810377

Cited by 34 publications

(15 citation statements)

References 18 publications

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“…Previous studies have shown that glycosaminoglycans and sulfated compounds inhibited many human lysosomal enzymes and bacterial sialidases [21–24]. In the present study, we found that sulfatide efficiently inhibited sialidase activities of influenza A virus NAs under conditions of less than pH 6.0.…”

Section: Discussionsupporting

confidence: 69%

Inhibition of influenza A virus sialidase activity by sulfatide

et al. 2003

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Sulfatide, which binds to in£uenza A viruses and prevents the viral infection, was found to inhibit the sialidase activities of in£uenza A viruses in a pH-dependent manner. The kinetic parameters of the e¡ect of sulfatide on the sialidase activities of human in£uenza A viruses using £uorometric assay indicated that sulfatide was a powerful and non-competitive type inhibitor in low-pH conditions. ß

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Section: Discussionsupporting

confidence: 69%

Inhibition of influenza A virus sialidase activity by sulfatide

et al. 2003

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“…Heavily sulfated mucins (sulfomucins) have many of the general lubricating and barrier functions of mucins with lower sulfate levels. There is accumulating evidence that sulfomucins may, in addition, rate-limit mucin degradation by mucin-degrading bacterial enzymes (4,7,13,15,18,24,26,27), and this role is thought to be particularly important in the colon, where approximately 10 14 bacterial cells are located (10). There have been reports of mucin-desulfating sulfatases that partially remove the sulfate from sulfomucin in a number of bacteria from the mouth, stomach, and colon and in feces.…”

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confidence: 99%

Cloning of a Mucin-Desulfating Sulfatase Gene from Prevotella Strain RS2 and Its Expression Using a Bacteroides Recombinant System

et al. 2000

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A gene encoding the mucin-desulfating sulfatase in Prevotella strain RS2 has been cloned, sequenced, and expressed in an active form. A 600-bp PCR product generated using primers designed from amino acid sequence data was used to isolate a 5,058-bp genomic DNA fragment containing the mucin-desulfating sulfatase gene. A 1,551-bp open reading frame encoding the sulfatase proprotein was identified, and the deduced 517-amino-acid protein minus its signal sequence corresponded well with the published mass of 58 kDa estimated by denaturing gel electrophoresis. The sulfatase sequence showed homology to aryl-and nonarylsulfatases with different substrate specificities from the sulfatases of other organisms. No sulfatase activity could be detected when the sulfatase gene was cloned into Escherichia coli expression vectors. However, cloning the gene into a Bacteroides expression vector did produce active sulfatase. This is the first mucin-desulfating sulfatase to be sequenced and expressed. A second open reading frame (1,257 bp) was identified immediately upstream from the sulfatase gene, coding in the opposite direction. Its sequence has close homology to iron-sulfur proteins that posttranslationally modify other sulfatases. By analogy, this protein is predicted to catalyze the modification of a serine group to a formylglycine group at the active center of the mucin-desulfating sulfatase, which is necessary for enzymatic activity.Mucins are high-molecular-weight glycoproteins which form the structural component of the protective mucus gel layer at the surfaces of the gastrointestinal, respiratory, and female genital tracts. Colonic mucin, particularly in the proximal region, contains significant levels of sulfate covalently bound to the mucin oligosaccharide chains, and levels of 2.0 to 6.5 g of sulfate per 100 g of mucin have been found (9, 17). Heavily sulfated mucins (sulfomucins) have many of the general lubricating and barrier functions of mucins with lower sulfate levels. There is accumulating evidence that sulfomucins may, in addition, rate-limit mucin degradation by mucin-degrading bacterial enzymes (4,7,13,15,18,24,26,27), and this role is thought to be particularly important in the colon, where approximately 10 14 bacterial cells are located (10). There have been reports of mucin-desulfating sulfatases that partially remove the sulfate from sulfomucin in a number of bacteria from the mouth, stomach, and colon and in feces. The effect of such sulfatases is to increase the susceptibility of the mucin to degradation by other mucin-degrading enzymes (4, 27). Elevated levels of bacterial mucin-desulfating sulfatases are found in feces of patients with ulcerative colitis (26). The sulfated sugar specificity of these fecal sulfatases, the number of different types present, the bacterial origin of the elevated levels, and the conditions which regulate bacterial production of such enzymes are unknown. The types of mucin-desulfating sulfatases that might be predicted include sulfatases specific for galactose-3-sulfate, g...

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“…The nature of this carbohydrate is of minor importance for the recognition by these enzymes, but large substituents on these carbohydrates make such compounds resistant towards bacterial and viral neuraminidases owing to steric hindrance (Drzeniek, 1973). However, we have observed that the chemically sulphated sialoglycopeptides inhibited the hydrolysis of N-acetylneuraminic acid from N-acetylneuraminyl-lactose, bovine submaxillarygland mucin and from the native sialoglycopeptides by steric hindrance (Mian et al, 1979). Vol.…”

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confidence: 60%