Glycan terminator

Paulson, James C.; Rademacher, Christoph

doi:10.1038/nsmb1109-1121

Cited by 22 publications

(16 citation statements)

References 12 publications

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“…GalNAc is typically present on O-glycans, and GlcNAc is normally a component of N-glycans. The binding of Sia to Gal or GalNAc requires a family of enzymes called sialyltransferases (ST), with each ST producing a specific linkage (Harduin-Lepers et al, 2005;Paulson and Rademacher, 2009;Xia et al, 2005). In some instances, multiple Sia may be linked together to form polysialic acid, most commonly in a a2-8 configuration (Hildebrandt et al, 2010).…”

Section: Sialic Acid Structurementioning

confidence: 99%

The use of sialidase therapy for respiratory viral infections

2013

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DAS181 is an inhaled bacterial sialidase which functions by removing sialic acid (Sia) from the surface of epithelial cells, preventing attachment and subsequent infection by respiratory viruses that utilize Sia as a receptor. DAS181 is typical of bacterial sialidases in cleaving Sia α2-3 and Sia α2-6 linkages, and it also has a demonstrated effect against acetylated and hydroxylated forms of Sia. The potency of the compound has been enhanced by coupling the active sialidase with an amphiregulin tag, allowing a longer duration of action and minimizing spread to the systemic circulation. DAS181 is now in Phase II development for the treatment of influenza, and it has also demonstrated activity in individual cases of parainfluenza in immunosuppressed patients. Continued evaluation of the roles and activities of bacterial sialidases is required to expand the range of successful antiviral therapies targeting Sia or its derivatives.

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Section: Sialic Acid Structurementioning

confidence: 99%

The use of sialidase therapy for respiratory viral infections

2013

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“…These protein-or lipid-linked ␣2,3-, ␣2,6-, and ␣2,8-sialosides are generated enzymatically by the cumulative actions of 20 different sialyltransferases, which all use CMP-NeuAc as their common donor substrate (12). Importantly, because of differences in acceptor substrate specificity and gene expression patterns of these related enzymes, cells and tissues display unique sialoside structures, which can have important functional consequences (13)(14)(15).…”

mentioning

confidence: 99%

Systemic Blockade of Sialylation in Mice with a Global Inhibitor of Sialyltransferases

Macauley

Arlian

Rillahan

et al. 2014

Journal of Biological Chemistry

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Background:In vivo pharmacological inhibition of sialyltransferases has, to date, not been possible. Results: 3F-NeuAc acts as a global sialyltransferase inhibitor in mice and causes kidney and liver dysfunction. Conclusion: Sialoside expression can be modulated in vivo with a sialyltransferase inhibitor. Significance: Pharmacological blockade of sialoside expression will be an important tool for future exploration of sialic acid in health and disease.

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“…A disulfide bond stabilizing the L- and the S-motifs is also conserved among these sialyltransferases (Datta et al 2001). Site-directed mutagenesis and structures of porcine ST3Gal-I show that the L-motif is involved in the donor binding, motifs 3 and VS contribute to the binding of the acceptor, and the S-motif participates in the binding of both donor and acceptor substrates (Datta 2009; Audry et al 2011; Rao et al 2009; Paulson and Rademacher 2009). A conserved histidine residue located in the VS-motif has been identified as the catalytic base from the x-ray crystal structures of porcine ST3Gal-I which have the GT-A fold with a single Rossmann domain (Rao et al 2009).…”

Section: Sialyltransferasesmentioning

confidence: 99%

Sialic acid metabolism and sialyltransferases: natural functions and applications

Chen

2012

Appl Microbiol Biotechnol

219

195

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Sialic acids are a family of negatively charged monosaccharides which are commonly presented as the terminal residues in glycans of the glycoconjugates on eukaryotic cell surface or as components of capsular polysaccharides or lipooligosaccharides of some pathogenic bacteria. Due to their important biological and pathological functions, the biosynthesis, activation, transfer, breaking down, and recycle of sialic acids are attracting increasing attention. The understanding of the sialic acid metabolism in eukaryotes and bacteria leads to the development of metabolic engineering approaches for elucidating the important functions of sialic acid in mammalian systems and for large-scale production of sialosides using engineered bacterial cells. As the key enzymes in biosynthesis of sialylated structures, sialyltransferases have been continuously identified from various sources and characterized. Protein crystal structures of seven sialyltransferases have been reported. Wild-type sialyltransferases and their mutants have been applied with or without other sialoside biosynthetic enzymes for producing complex sialic acid-containing oligosaccharides and glycoconjugates. This mini-review focuses on current understanding and applications of sialic acid metabolism and sialyltransferases.

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Glycan terminator

Cited by 22 publications

References 12 publications

The use of sialidase therapy for respiratory viral infections

The use of sialidase therapy for respiratory viral infections

Systemic Blockade of Sialylation in Mice with a Global Inhibitor of Sialyltransferases

Sialic acid metabolism and sialyltransferases: natural functions and applications

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