Chemoenzymatic synthesis of ring 18O-labeled sialic acid

2008 ◽  
Vol 86 (11) ◽  
pp. 1005-1009 ◽  
Author(s):  
Deepani Indurugalla ◽  
Andrew J Bennet
Keyword(s):  
Sialic Acid ◽  
Functional Group ◽  
Chemoenzymatic Synthesis ◽  
Hydroxyl Group ◽  
Synthetic Route ◽  
Acetylneuraminic Acid ◽  
O 18 ◽  
Sialic Acid Aldolase

Methyl 4,6-O-benzylidene-α-D-glucopyranoside was converted into methyl 2-azido-2-deoxy-4,6-O-benzylidene-α-D-altropyranoside via a synthetic route that incorporated two inversions of configuration. Activation of the C-3 hydroxyl group as a triflate ester followed by an SN2 reaction with O-18 labeled benzoate gave, after standard functional group manipulations, 2-acetamido-2-deoxy-D-(3-18O)mannose. Coupling of the labeled N-acetyl-mannosamine with pyruvate was catalyzed by sialic acid aldolase to give ring-oxygen-labeled sialic acid in an overall yield of 11.4% over 10 steps.Key words: N-acetylneuraminic acid, sialic acid oxygen-18, chemoenzymatic.

Structural determination of the polysaccharide antigens of Neisseria meningitidis serogroups Y, W-135, and BO

1976 ◽  
Vol 54 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Apurba K. Bhattacharjee ◽  
Harold J. Jennings ◽  
C. Paul Kenny ◽  
Adèle Martin ◽  
Ian C. P. Smith
Keyword(s):  
Sialic Acid ◽  
Acetyl Derivative ◽  
Major Product ◽  
Hydroxyl Group ◽  
Nmr Studies ◽  
Acetylneuraminic Acid ◽  
Nmr Data ◽  
Polysaccharide Antigens ◽  
C Nmr

The purified high molecular weight serogoup Y meningococcal polysaccharide contains equimolar proportions of D-glucose and N-acetylneuraminic acid and is partially O-acetylated. Carbon-13 nuclear magnetic resonance (NMR) studies, together with other chemical data, have indicated that the polysaccharide is linked only at C-6 of the D-glucose and C-4 of the sialic acid residues, all the linkages being in the α-configuration. The 13C NMR data also indicated that the Y polysaccharide is composed of an alternating sequence of these two different residues, and this was confirmed by its autohydrolysis where the major product was 4-O-α-D-glucopyranosyl-β-D-N-acetylneuraminic acid. The W-135 polysaccharide differs from that of Y only in the absence of O-acetylation and in the configuration of one hydroxyl group of the disaccharide repeating unit. In this case autohydrolysis yielded 4-O-α-D-galactopyranosyl-β-D-N-acetylneuraminic acid as the major product. Structural evidence indicates that the BO and Y polysaccharides are identical.Methanolysis of the Y polysaccharide yielded in addition to the methyl glycosides of glucose and sialic acid, a 9-O-acetyl derivative of the latter. This derivative was formed during the re-N-acetylation process and its formation was mainly due to the presence of sodium ions in the original polysaccharide.

scholarly journals The fate of orally administered sialic acid: First insights from patients with N-acetylneuraminic acid synthase deficiency and control subjects

2021 ◽  
Vol 28 ◽  
pp. 100777
Author(s):  
Christel Tran ◽  
Licia Turolla ◽  
Diana Ballhausen ◽  
Sandrine Cornaz Buros ◽  
Tony Teav ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Acetylneuraminic Acid ◽  
Control Subjects ◽  
And Control

scholarly journals Modulation of Substrate Specificities of d-Sialic Acid Aldolase through Single Mutations of Val-251

2011 ◽  
Vol 286 (16) ◽  
pp. 14057-14064 ◽  
Author(s):  
Chien-Yu Chou ◽  
Tzu-Ping Ko ◽  
Kuan-Jung Wu ◽  
Kai-Fa Huang ◽  
Chun-Hung Lin ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Substrate Specificities ◽  
Sialic Acid Aldolase

scholarly journals N-Glycolylneuraminic Acid in Animal Models for Human Influenza A Virus

Viruses ◽  
2021 ◽  
Vol 13 (5) ◽  
pp. 815
Author(s):  
Cindy M. Spruit ◽  
Nikoloz Nemanichvili ◽  
Masatoshi Okamatsu ◽  
Hiromu Takematsu ◽  
Geert-Jan Boons ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Animal Models ◽  
Influenza A ◽  
Influenza Virus Infection ◽  
Influenza Viruses ◽  
Upper Respiratory Tract ◽  
Human Influenza ◽  
Influenza A Viruses ◽  
Sialic Acid Content ◽  
Acetylneuraminic Acid

The first step in influenza virus infection is the binding of hemagglutinin to sialic acid-containing glycans present on the cell surface. Over 50 different sialic acid modifications are known, of which N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc) are the two main species. Animal models with α2,6 linked Neu5Ac in the upper respiratory tract, similar to humans, are preferred to enable and mimic infection with unadapted human influenza A viruses. Animal models that are currently most often used to study human influenza are mice and ferrets. Additionally, guinea pigs, cotton rats, Syrian hamsters, tree shrews, domestic swine, and non-human primates (macaques and marmosets) are discussed. The presence of NeuGc and the distribution of sialic acid linkages in the most commonly used models is summarized and experimentally determined. We also evaluated the role of Neu5Gc in infection using Neu5Gc binding viruses and cytidine monophosphate-N-acetylneuraminic acid hydroxylase (CMAH)-/- knockout mice, which lack Neu5Gc and concluded that Neu5Gc is unlikely to be a decoy receptor. This article provides a base for choosing an appropriate animal model. Although mice are one of the most favored models, they are hardly naturally susceptible to infection with human influenza viruses, possibly because they express mainly α2,3 linked sialic acids with both Neu5Ac and Neu5Gc modifications. We suggest using ferrets, which resemble humans closely in the sialic acid content, both in the linkages and the lack of Neu5Gc, lung organization, susceptibility, and disease pathogenesis.

Interaction of Mycoplasma gallisepticum with sialyl glycoproteins

1980 ◽  
Vol 30 (2) ◽  
pp. 353-361
Author(s):  
L R Glasgow ◽  
R L Hill
Keyword(s):  
Sialic Acid ◽  
Mycoplasma Gallisepticum ◽  
Binding Assays ◽  
Molecular Weights ◽  
Acetylneuraminic Acid ◽  
Direct Binding ◽  
Membrane Bound ◽  
Strict Specificity ◽  
Human Glycophorin ◽  
Acid Structure

The binding of several glycoproteins to freshly grown and harvested cells of Mycoplasma gallisepticum was examined. Only human glycophorin, the major sialoglycoprotein of the erythrocyte membrane, bound tightly as judged by direct binding assays with 125I-labeled glycoproteins. Neuraminidase-treated glycophorin did not bind, suggesting that binding is mediated through sialic acid groups. Although other sialoglycoproteins did not appear to bind M. gallisepticum by direct binding assays, some inhibited the binding of glycophorin. The best inhibitors had a mucin-like structure, with high molecular weights and high sialic acid contents. N-acetylneuraminic acid appeared to be the favored sialic acid structure for binding, but there was no strict specificity for its anomeric linkage. Neuraminidase activity could not be detected on the surface of M. gallisepticum, suggesting that this enzyme is not involved in the mechanism of adherence of sialoglycoproteins. Binding of sialoglycoproteins was time dependent, however, and markedly diminished with increasing ionic strength, but was largely unaffected between pH 4 and 9.

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