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Showing 1–13 of 13 results
Advanced filters: Author: Ethan D. Goddard-Borger Clear advanced filters

  • Pseudaminic acids (Pse) are a family of carbohydrates found within bacterial lipopolysaccharides, capsular polysaccharides and glycoproteins. Now, monoclonal antibodies have been developed that recognize diverse Pse across several bacterial species, enabling mapping of the Pse glycoproteome and demonstrating therapeutic potential against multidrug-resistant Acinetobacter baumanii in in vitro and in vivo infection models.

    • Arthur H. Tang
    • Niccolay Madiedo Soler
    • Richard J. Payne
    Research
    Nature Chemical Biology
    P: 1-12

  • Here, Lopaticki et al. show that Plasmodium falciparum expresses a Dpy19 C-mannosyltransferase in the endoplasmic reticulum that glycosylates TSR domains. Functional characterization shows that PfDpy19 plays a critical role in transmission through mosquitoes as PfDpy19-deficiency abolishes C-glycosylation and destabilizes proteins relevant for gametogenesis and oocyst formation.

    • Sash Lopaticki
    • Robyn McConville
    • Justin A. Boddey
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-18

  • Proteolytic maturation of an important transcriptional regulator is performed by a glycosyltransferase. The reaction involves glycosylation of a glutamate residue and conversion of the γ-glycosyl ester product into an N-acyl pyroglutamate, which undergoes spontaneous hydrolysis to effect peptide backbone fission.

    • Ethan D Goddard-Borger
    News & Views
    Nature Chemical Biology
    Volume: 12, P: 892-893

  • Trefoil factors (TFFs) protect the mucosa and have various reported binding activities, but whether they share a common interaction mechanism has remained unclear. Here, the authors provide structural and biochemical evidence that all three human TFFs are divalent lectins that recognise the same disaccharide.

    • Michael A. Järvå
    • James P. Lingford
    • Ethan D. Goddard-Borger
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-9

  • The tunicamycins, secondary metabolites of various Streptomyces species, are invaluable tools in glycobiology. It has now been shown that their biosynthesis involves an unusual exo-glycal intermediate produced by previously unknown short-chain dehydrogenase/reductase activity.

    • Ethan D. Goddard-Borger
    • Stephen G. Withers
    News & Views
    Nature Chemistry
    Volume: 4, P: 520-521

  • Conjugation of a known, mechanism-based glycosidase inhibitor to sensitive fluorophores yielded unexpectedly potent and selective probes for quantifying active lysosomal glucocerebrosidase. These conjugates could prove to be invaluable tools for diagnosing and studying Gaucher disease.

    • Ethan D Goddard-Borger
    • Tom Wennekes
    • Stephen G Withers
    News & Views
    Nature Chemical Biology
    Volume: 6, P: 881-883

  • YihQ hydrolyzes the glycosidic linkage in sulfoquinovosyl diacylglyceride (SQDG) to form sulfoquinovose (SQ). Crystal structure analysis reveals active site residues required for the specificity of YihQ for SQ and allows the identification of other YihQ homologs.

    • Gaetano Speciale
    • Yi Jin
    • Ethan D Goddard-Borger
    Research
    Nature Chemical Biology
    Volume: 12, P: 215-217

  • An engineered Pichia pastoris strain enables the synthesis of tryptophan C-mannosylated proteins, and selected monoclonal antibodies provide tools for detecting these modified proteins and studying their functions.

    • Alan John
    • Michael A. Järvå
    • Ethan D. Goddard-Borger
    Research
    Nature Chemical Biology
    Volume: 17, P: 428-437

  • Tryptophan C-mannosyltransferase (CMT) enzymes append a mannose to the first tryptophan of select sequences, which is important for the trafficking, folding and function of secretory and transmembrane proteins involved in cellular communication processes. A study reveals the structure, mode of peptide recognition and catalytic mechanism for the eukaryotic C-mannosyltransferase DPY19.

    • Joël S. Bloch
    • Alan John
    • Kaspar P. Locher
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 19, P: 575-584

  • The role of O-glycosylation in the malaria life cycle is largely unknown. Here, the authors identify a Plasmodium protein O-fucosyltransferase and show that it is important for normal trafficking of a subset of surface proteins, particularly CSP and TRAP, and efficient infection of mosquito and vertebrate hosts.

    • Sash Lopaticki
    • Annie S. P. Yang
    • Justin A. Boddey
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-10

  • Crystal structures of α-L-iduronidase, the enzyme linked to MPS I, now provide snapshots of the catalytic pathway and rationalize the role of 100 disease-related mutations, while biochemical analysis of deglycosylated and mutated enzymes define roles for non–active site residues in controlling function.

    • Haiying Bie
    • Jiang Yin
    • Michael N G James
    Research
    Nature Chemical Biology
    Volume: 9, P: 739-745