Abstract:Many viruses achieve reversible attachment to sialic acid (Sia) by encoding envelope glycoproteins with receptor-binding and receptor-destroying activities. Toroviruses and group 2 coronaviruses bind to O-acetylated Sias, presumably via their spike proteins (S), whereas other glycoproteins, the hemagglutinin-esterases (HE), destroy Sia receptors by de-O-acetylation. Here, we present a comprehensive study of these enzymes. Sialate-9-O-acetylesterases specific for 5-N-acetyl-9-Oacetylneuraminic acid, described f… Show more
“…This has also been reported from the rat liver esterase [46]. Only the esterase from bovine toroviruses hydrolyses a Sia with a 7-O-acetyl group, since it seems to prefer Sia di-O-acetylated at C-7 or C-8 and at C-9 of its side chain [29]. An explanation for Fig.…”
Section: Discussionmentioning
confidence: 62%
“…In contrast to these eukaryotic enzymes a variety of viruses were found to exhibit sialate esterase activities strongly specific for either 4-O-acetyl or 9-O-acetyl groups, respectively [28][29][30][31]. These Sia have receptor functions for these viruses.…”
Section: Discussionmentioning
confidence: 93%
“…The first example was the 9-O-acetyl-specific esterase isolated from influenza C virus and considered as a "receptor-destroying" enzyme [27,28]. Since then besides this orthomyxovirus such esterases were discovered in a variety of corona-and toroviruses, which preferentially hydrolyse either the 4-or 9-mono-O-acetylated or the sidechain di-O-acetylated Sia [29]. Several of these enzymes were cloned [30,31].…”
Sialate-O-acetylesterase was purified almost 900-fold from particle-free supernatants of horse liver by gel filtration, ion-exchange chromatography and isoelectric focussing. The native enzyme on gel filtration exhibits a molecular weight of 54,000 Da. It was separated by isoelectric focussing into two forms with pI values of 4.8 and 5.7, respectively. The esterase with a lower pI hydrolyses only 9-O-acetyl groups from sialic acids (K(M) 1.1 mM), while that with the higher pI esterifies both 4- and 9-O-acetylated monosaccharides at similar rates (K(M) 0.3 M and 1.3 mM, respectively). Both forms are inactive with 7-O-acetylated N-acetylneuraminic acid. Enzyme assays were carried out at the pH optimum (pH 8.4-8.6) using free O-acetylated sialic acids followed by direct analysis of the reaction products by isocratic anion-exchange HPLC. Glycosidically bound sialic acids can also be de-O-acetylated. Horse liver esterase seems to be an essential enzyme for the catabolism of 4-O-acetylated sialoglycoconjugates, since sialidase from this tissue cannot act on 4-O-acetylated sialic acids.
“…This has also been reported from the rat liver esterase [46]. Only the esterase from bovine toroviruses hydrolyses a Sia with a 7-O-acetyl group, since it seems to prefer Sia di-O-acetylated at C-7 or C-8 and at C-9 of its side chain [29]. An explanation for Fig.…”
Section: Discussionmentioning
confidence: 62%
“…In contrast to these eukaryotic enzymes a variety of viruses were found to exhibit sialate esterase activities strongly specific for either 4-O-acetyl or 9-O-acetyl groups, respectively [28][29][30][31]. These Sia have receptor functions for these viruses.…”
Section: Discussionmentioning
confidence: 93%
“…The first example was the 9-O-acetyl-specific esterase isolated from influenza C virus and considered as a "receptor-destroying" enzyme [27,28]. Since then besides this orthomyxovirus such esterases were discovered in a variety of corona-and toroviruses, which preferentially hydrolyse either the 4-or 9-mono-O-acetylated or the sidechain di-O-acetylated Sia [29]. Several of these enzymes were cloned [30,31].…”
Sialate-O-acetylesterase was purified almost 900-fold from particle-free supernatants of horse liver by gel filtration, ion-exchange chromatography and isoelectric focussing. The native enzyme on gel filtration exhibits a molecular weight of 54,000 Da. It was separated by isoelectric focussing into two forms with pI values of 4.8 and 5.7, respectively. The esterase with a lower pI hydrolyses only 9-O-acetyl groups from sialic acids (K(M) 1.1 mM), while that with the higher pI esterifies both 4- and 9-O-acetylated monosaccharides at similar rates (K(M) 0.3 M and 1.3 mM, respectively). Both forms are inactive with 7-O-acetylated N-acetylneuraminic acid. Enzyme assays were carried out at the pH optimum (pH 8.4-8.6) using free O-acetylated sialic acids followed by direct analysis of the reaction products by isocratic anion-exchange HPLC. Glycosidically bound sialic acids can also be de-O-acetylated. Horse liver esterase seems to be an essential enzyme for the catabolism of 4-O-acetylated sialoglycoconjugates, since sialidase from this tissue cannot act on 4-O-acetylated sialic acids.
“…Furthermore, a regulatory influence of these two enzymes on the expression of Neu5,9Ac 2 in E. coli [12] and group B Streptococcus [19] has been discussed. Sialate-O-acetylesterases have frequently been detected in animals of the deuterostome lineage, in bacteria and in viruses, some of which were partly or totally purified and the respective genes cloned [20][21][22][23][24]. The techniques of the analysis of SOAE activities will therefore be included.…”
The O-acetylation of sialic acids is one of the most frequent modifications of these monosaccharides and modulates many cell biological and pathological events. Sialic acid-specific O-acetyltransferases and O-acetylesterases are responsible for the metabolism of esterified sialic acids. Assays were developed for the analysis of the activities and specificities of these enzymes. The methods had to be varied in dependence on the substrate assayed, the kind of biological source, and the state of enzyme purity. With the new techniques the primary site of O-acetyl incorporation at C-7, catalyzed by the animal sialate-O-acetyltransferases studied, was ascertained. Correspondingly, this enzyme, for example from bovine submandibular gland, can be denominated as AcCoA:sialate-7-O-acetyltransferase (EC 2.3.1.45). Methods for assaying the activity of esterases de-O-acetylating sialic acids and their metabolic cooperation with the O-acetyltransferases are presented.
“…Therefore O-acetylated gangliosides could serve as targets for directed cancer therapies. O-Acetylation has contrasting effects on the process of viral attachment to membrane-bound sialoglycans; this is an obligatory modification for the association of some enteric and respiratory viruses but inhibits binding by others (8,9). As a final example, the sialylated polysaccharide capsules of group B Streptococcus (10), Escherichia coli K1 (11,12), and Neisseria meningitidis serogroups C, W-135, and Y (13) have been shown to be O-acetylated in some cases, which results in altered immunogenic properties.…”
We have identified a sialate O-acetyltransferase in the lipo-oligosaccharide biosynthesis locus of Campylobacter jejuni. Strains possessing this locus are known to produce sialylated outer core structures that mimic host gangliosides, and have been implicated in triggering the onset of Guillain-Barré syndrome. The acetyltransferase, which was cloned and expressed as a fusion construct in Escherichia coli, is soluble and homologous with members of the NodL-LacA-CysE family of O-acetyltransferases. This enzyme catalyzes the transfer of O-acetyl groups onto oligosaccharide-bound sialic acid, with a high specificity for terminal ␣2,8-linked residues. The modification is directed to C-9 and not C-7 as is believed to occur more commonly in other organisms. Despite their wide prevalence and importance in both eukaryotes and prokaryotes, this is the first report to describe the characterization of a purified sialate O-acetyltransferase.
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