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| Open AccessUnravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus
The mucus layer is an important physical niche within the gut which harbours a distinct microbial community. Here the authors show that specific carbohydrate-binding modules associated with bacterial carbohydrate-active enzymes are mucus adhesins that target regions of the distal colon rich in sialomucins.
- C. David Owen
- , Louise E. Tailford
- & Nathalie Juge
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Article
| Open AccessLipoteichoic acid deficiency permits normal growth but impairs virulence of Streptococcus pneumoniae
Teichoic acid is bound to peptidoglycan (wall teichoic acid, WTA) or to membrane glycolipids (lipoteichoic acid, LTA) in most Gram-positive bacteria. Here, the authors identify a putative ligase required for the assembly of LTA, but not WTA, and important for Streptococcus pneumoniae virulence in mouse models.
- Nathalie Heß
- , Franziska Waldow
- & Nicolas Gisch
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Article
| Open AccessRoles of two types of heparan sulfate clusters in Wnt distribution and signaling in Xenopus
Wnt proteins mediate embryonic development but how protein localization and patterning is regulated is unclear. Here, the authors show that distinct structures with different heparan sulfate modifications (‘N-sulfo-rich’ and ‘N-acetyl-rich’) regulate cellular localization and signal transduction of Wnt8 in Xenopus.
- Yusuke Mii
- , Takayoshi Yamamoto
- & Masanori Taira
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Article
| Open AccessThe interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences
GalNAc transferases’ (GalNAc-Ts) catalytic domains are connected to a lectin domain through a flexible linker. Here the authors present a structural analysis of GalNAc-T4 that implicates the linker region as modulator of the orientations of the lectin domain, which in turn imparts substrate specificity.
- Matilde de las Rivas
- , Erandi Lira-Navarrete
- & Ramon Hurtado-Guerrero
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Article
| Open AccessCarrageenan catabolism is encoded by a complex regulon in marine heterotrophic bacteria
Carrageenans, major cell wall polysaccharides of red macroalgae, are metabolised by marine heterotrophic bacteria through unclear mechanisms. Here, the authors identify an unusual polysaccharide-utilization locus encoding carrageenan catabolism in a marine bacterium, and characterise the complete pathway.
- Elizabeth Ficko-Blean
- , Aurélie Préchoux
- & Gurvan Michel
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Article
| Open AccessO-GlcNAcylation of SIRT1 enhances its deacetylase activity and promotes cytoprotection under stress
SIRT1 is a stress sensor whose deacetylase activity is increased during cellular stress, but the molecular mechanism is unclear. Here, the authors show that O-GlcNAcylation of SIRT1 is elevated upon different stress stimuli and increases SIRT1 deacetylase activity, protecting cells from stress-induced apoptosis.
- Cuifang Han
- , Yuchao Gu
- & Wengong Yu
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Article
| Open AccessNetwork inference from glycoproteomics data reveals new reactions in the IgG glycosylation pathway
IgG glycosylation is an important factor in immune function, yet the molecular details of protein glycosylation remain poorly understood. The data-driven approach presented here uses large-scale plasma IgG mass spectrometry measurements to infer new biochemical reactions in the glycosylation pathway.
- Elisa Benedetti
- , Maja Pučić-Baković
- & Jan Krumsiek
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Article
| Open AccessStructural and electronic determinants of lytic polysaccharide monooxygenase reactivity on polysaccharide substrates
Copper-dependent lytic polysaccharide monooxygenases (LPMOs) oxidatively cleave polysaccharides. Here the authors present a structure-function characterization of fungal LPMOs, showing that a particular LPMO cleaves xylan using a mechanism that involves an alternative copper coordination geometry.
- T. J. Simmons
- , K. E. H. Frandsen
- & P. Dupree
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Article
| Open AccessStructural insights into the substrate binding adaptability and specificity of human O-GlcNAcase
O-linked β-N-acetyl glucosamine (O-GlcNAc) is an important protein modification that is hydrolyzed by O-GlcNAcase (OGA). Here the authors give insights into OGA substrate recognition by presenting four human OGA structures complexed with glycopeptide substrates containing a single O-GlcNAc modification on either a serine or threonine.
- Baobin Li
- , Hao Li
- & Jiaoyang Jiang
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Article
| Open AccessHeparan sulfate proteoglycans present PCSK9 to the LDL receptor
PCSK9 interacts with LDL receptor, causing its degradation, and consequently reduces the clearance of LDL. Here, Gustafsen et al. show that PCSK9 interacts with heparan sulfate proteoglycans and this binding favors LDLR degradation. Pharmacological inhibition of this binding can be exploited as therapeutic intervention to lower LDL levels.
- Camilla Gustafsen
- , Ditte Olsen
- & Simon Glerup
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Article
| Open AccessStructural basis of Notch O-glucosylation and O–xylosylation by mammalian protein–O-glucosyltransferase 1 (POGLUT1)
POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors. Here the authors report the structure of human POGLUT1 in complexes with 3 different EGF-like domains and donor substrates and shed light on the enzyme’s substrate specificity and catalytic mechanism
- Zhijie Li
- , Michael Fischer
- & James M. Rini
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Article
| Open AccessAn engineered high affinity Fbs1 carbohydrate binding protein for selective capture of N-glycans and N-glycopeptides
Protein glycosylation is an essential post-translational modification which analysis is complicated by the diversity of glycan composition and heterogeneity at individual attachment sites. Here the authors describe a method to selectively enrich N-linked glycopeptides to facilitate the detection of micro-heterogeneity in N-glycosylation.
- Minyong Chen
- , Xiaofeng Shi
- & James C. Samuelson
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Article
| Open AccessHybrid mass spectrometry approaches in glycoprotein analysis and their usage in scoring biosimilarity
Many biopharmaceuticals exhibit mixed heterogeneity in their post-translational modifications (PTMs) that are essential for their function. Here the authors use a combination of mass spectrometry techniques to analyse human erythropoietin (EPO) and properdin to discover new PTMs on properdin and derive a biosimilarity score for various sources of EPO.
- Yang Yang
- , Fan Liu
- & Albert J. R. Heck
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Article
| Open AccessMultivalent display of minimal Clostridium difficile glycan epitopes mimics antigenic properties of larger glycans
Immunologically-active glycans are promising vaccine candidates but can be difficult to synthesize. Here, the authors show that pentavalent display of a minimal disaccharde epitope on a chemical scaffold can mimic a native C. difficileglycan antigen, representing a simple approach to synthetic vaccine production.
- Felix Broecker
- , Jonas Hanske
- & Peter H. Seeberger