Glycoconjugates articles within Nature Communications

Featured

  • Article
    | Open Access

    O-acetylation is a common modification of sialic acids. Here, a library of synthetic O-acetylated sialosides made it possible to develop an ion mobility mass spectrometry (IM-MS) approach that can elucidate exact O-acetylation patterns and glycosidic linkage types of sialosides isolated from biological samples.

    • Gaёl M. Vos
    • , Kevin C. Hooijschuur
    •  & Geert-Jan Boons
  • Article
    | Open Access

    Heparan sulfate (HS) and chondroitin sulfate (CS) are different glycosaminoglycan chains that are attached to core proteins via the same linker tetrasaccharide, and it was unclear how core proteins are specifically modified with HS or CS. Here, the authors determine that the CS-initiating glycosyltransferase CSGALNACT2 is promiscuous, whereas the HS-initiating glycosyltransferase EXTL3 selects only certain core proteins for modification.

    • Douglas Sammon
    • , Anja Krueger
    •  & Erhard Hohenester
  • Article
    | Open Access

    Cellular glycosylation is complex and heterogeneous, which is challenging to reproduce synthetically. Here, the authors report on enzymatic remodelling of multivalent glycosylated bacteriophages to produce genetically encoded library of N-glycans which can be used to measure glycan-protein interactions with lectins on the surface of live cells and organs.

    • Chih-Lan Lin
    • , Mirat Sojitra
    •  & Ratmir Derda
  • Article
    | Open Access

    Access to glycoenzymes for basic and applied research is limited by difficulties with their recombinant expression. Here, the authors describe a universal strategy for converting membrane-bound glycosyltransferases into water-soluble biocatalysts, which are expressed at high levels with retention of activity.

    • Thapakorn Jaroentomeechai
    • , Yong Hyun Kwon
    •  & Matthew P. DeLisa
  • Article
    | Open Access

    AM0627 is a bis-O-glycan mucinase that might work in the final steps of mucus degradation, thereby providing a carbon and nitrogen source for Akkermansia muciniphila. Here, the authors provide molecular insights into AM0627 function from X-ray crystallography and computer simulations.

    • Víctor Taleb
    • , Qinghua Liao
    •  & Ramon Hurtado-Guerrero
  • Article
    | Open Access

    Here, Broszeit et al. show that circulating A/H3N2 viruses have evolved binding specificity to α2,6-sialosides on extended LacNAc moieties and therefore cannot agglutinate erythrocytes. Applying glycan remodeling allows to install functional receptors on erythrocytes and promotes identification of newly circulating variants to facilitate vaccine design.

    • Frederik Broszeit
    • , Rosanne J. van Beek
    •  & Geert-Jan Boons
  • Article
    | Open Access

    Sialic acid-binding immunoglobulin-type lectins (Siglecs) are a family of immunomodulatory receptors expressed on cells of the hematopoietic lineage. Here the authors demonstrate an approach for the identification of the glycan ligands of Siglecs, which is also applicable to other families of glycan-binding proteins.

    • Emily Rodrigues
    • , Jaesoo Jung
    •  & Matthew S. Macauley
  • Article
    | Open Access

    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
  • Article
    | Open Access

    Core-fucosylation of the N-glycan core is an essential biological modification and the α1,6- fucosyltransferase FUT8 is the only enzyme in humans that catalyses this modification through the addition of an α-1,6-linked fucose to N-glycans. Here the authors provide insights into FUT8 substrate recognition by determining the 1.95 Å crystal structure of human FUT8 complexed with GDP and a biantennary complex N-glycan.

    • Ana García-García
    • , Laura Ceballos-Laita
    •  & Ramon Hurtado-Guerrero
  • Article
    | Open Access

    The glycome of parasites can have immunomodulatory properties or help to avoid immune surveillance, but details are unknown. Here, Martini et al. characterize the N-glycome of the canine heartworm, reveal an unprecedented complexity, particularly in anionic N-glycans, and determine recognition by components of the immune system.

    • Francesca Martini
    • , Barbara Eckmair
    •  & Katharina Paschinger
  • Article
    | Open Access

    Melioidosis and glanders are multifaceted infections caused by gram-negative bacteria. Here, the authors synthesize a series of oligosaccharides that mimic the lipopolysaccharides present on the pathogens’ surface and use them to develop novel glycoconjugates for vaccine development.

    • Marielle Tamigney Kenfack
    • , Marcelina Mazur
    •  & Charles Gauthier
  • Article
    | Open Access

    Arabinogalactan forms parts of the cellular envelope ofMycobacterium tuberculosis, however due to its size chemical synthesis is a massive task. Here the authors report the synthesis of branched heneicosafuranosyl arabinogalactan fragment by repeated use of a Au/Ag-catalysed glycosylation methodology.

    • Shivaji A. Thadke
    • , Bijoyananda Mishra
    •  & Srinivas Hotha
  • Article |

    Inhibiting the interaction between the membrane protein P-selectin and its ligand PSGL-1 is thought to block inflammation. Here the authors report an efficient stereoselective synthesis for PSGL-1 glycopeptide mimics and show that these compounds inhibit PSGL-1/P-selectin in vitro and in vivo.

    • Venkata R. Krishnamurthy
    • , Mohammed Y. R. Sardar
    •  & Elliot L. Chaikof