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| Open AccessOrigins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation
Streptococcal siglec-like binding regions (SLBRs) selectively bind cell surface glycans, but the basis for this selectivity is not understood. Here, the authors identify selectivity-modulating SLBR regions and study how changes in SLBR glycan selectivity affect interactions with human glycoprotein receptors.
- Barbara A. Bensing
- , Haley E. Stubbs
- & T. M. Iverson
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Article
| Open AccessTrefoil factors share a lectin activity that defines their role in mucus
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
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Article
| Open AccessLiquid-liquid phase separation and extracellular multivalent interactions in the tale of galectin-3
Galectin-3 consists of an unstructured N-terminal domain (NTD) and a structured carbohydrate-recognition domain and agglutinates neutrophils and glycosylated molecules in the extracellular milieu. Here the authors combine biophysical and biochemical experiments with NMR measurements and show that the galectin-3 NTD undergoes liquid-liquid phase separation (LLPS) and agglutinates other molecules through this process.
- Yi-Ping Chiu
- , Yung-Chen Sun
- & Jie-rong Huang
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Article
| 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 AccessThe fungal-specific β-glucan-binding lectin FGB1 alters cell-wall composition and suppresses glucan-triggered immunity in plants
β-glucans derived from fungal cell walls can trigger immune responses in animals, yet their roles in plant-fungal interactions are less well known. Here, Wawraet al. show that the FGB1 proteins, secreted by the fungal endophyte P. indica, can alter fungal cell wall composition and suppress immune responses in plants.
- Stephan Wawra
- , Philipp Fesel
- & Alga Zuccaro
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Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions
Galectin-1 (GAL1) is a secreted protein that binds to glycans and to the pre-B-cell receptor (pre-BCR). Here Bonzi et al. show that pre-BCR binding to GAL1 causes a conformational change in the GAL1 carbohydrate-binding site to inhibit binding to selected glycans.
- Jeremy Bonzi
- , Olivier Bornet
- & Latifa Elantak