A Sweet Coating—How Bacteria Deal with Sugars

Corfield, Anthony P.; Wiggins, Rebecca; Edwards, Cathryn; Myerscough, Neil; Warren, Bryan F.; Soothill, Peter; Millar, Michael; Horner, Patrick J

doi:10.1007/978-1-4615-0065-0_1

Cited by 14 publications

(9 citation statements)

References 52 publications

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“…These glycans are often exploited by pathogens to facilitate colonization and disease (46,48,49). The expression and glycosylation of mucins differ depending on a number of factors, including the species, the location within the body, inflammation, and the presence of microbes (48,50,51). To further the study of bacterial interactions with complex glycoproteins, a mucin microarray was developed containing a wide range of natural mucins, including those from a number of gastrointestinal sites in several animal species (22).…”

Section: Discussionmentioning

confidence: 99%

Divergent Mechanisms of Interaction of Helicobacter pylori and Campylobacter jejuni with Mucus and Mucins

et al. 2013

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f Helicobacter pylori and Campylobacter jejuni colonize the stomach and intestinal mucus, respectively. Using a combination of mucus-secreting cells, purified mucins, and a novel mucin microarray platform, we examined the interactions of these two organisms with mucus and mucins. H. pylori and C. jejuni bound to distinctly different mucins. C. jejuni displayed a striking tropism for chicken gastrointestinal mucins compared to mucins from other animals and preferentially bound mucins from specific avian intestinal sites (in order of descending preference: the large intestine, proximal small intestine, and cecum). H. pylori bound to a number of animal mucins, including porcine stomach mucin, but with less avidity than that of C. jejuni for chicken mucin. The strengths of interaction of various wild-type strains of H. pylori with different animal mucins were comparable, even though they did not all express the same adhesins. The production of mucus by HT29-MTX-E12 cells promoted higher levels of infection by C. jejuni and H. pylori than those for the non-mucus-producing parental cell lines. Both C. jejuni and H. pylori bound to HT29-MTX-E12 mucus, and while both organisms bound to glycosylated epitopes in the glycolipid fraction of the mucus, only C. jejuni bound to purified mucin. This study highlights the role of mucus in promoting bacterial infection and emphasizes the potential for even closely related bacteria to interact with mucus in different ways to establish successful infections.

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Section: Discussionmentioning

confidence: 99%

Divergent Mechanisms of Interaction of Helicobacter pylori and Campylobacter jejuni with Mucus and Mucins

et al. 2013

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“…To colonise mucosal surfaces and invade the epithelium, microbes commonly interact with glycan structures of the host glycocalyx 11 16. Bacterial fimbriae (or pili), various outer membrane proteins and cell wall components—for example, lipopolysaccharides (LPSs)—may all function as adhesins.…”

Section: Mucus Layer and Epithelial Glycocalyx As Barriers To Bacterimentioning

confidence: 99%

Sweet-talk: role of host glycosylation in bacterial pathogenesis of the gastrointestinal tract

Moran

Gupta

Joshi

2011

Gut

200

159

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Glycosylation is a key modification of proteins and lipids and is involved in most intermolecular and intercellular interactions. The gastrointestinal mucus gel is continuous and can be divided into two layers: a secreted loosely associated layer and a layer firmly attached to the mucosa. In addition, the membrane-bound glycosylated proteins and lipids create a glycocalyx, which remains adherent on each cell and is dynamic and responsive to the physiological state and environment of the cell. The secreted glycans form a mucus gel layer that serves as a physicochemical sensor and barrier network and is primarily composed of mucins and associated peptides.

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“…In the small intestine, the glycocalyx layer directly covers the entire surface of the epithelial cells [5][6][7] while the overlaying lubricant mucus layer is thin and discontinuous 7,8 . The glycocalyx comprises highly diverse glycoproteins and glycolipids expressed on the epithelial cell membrane, many of which serve as receptors for bacterial adhesion 7,[9][10][11] . The glycocalyx thus act as attachment sites for normal flora to limit colonization by pathogens, in addition to functioning as size-selective diffusion barrier to exclude deleterious bacteria and viruses [12][13][14] .…”

mentioning

confidence: 99%

“…Transmembrane mucins MUC1, MUC3, MUC4, MUC12, MUC13, and MUC17 are expressed by the intestinal mucosal epithelial cells and are presumed to be the main components of the glycocalyx 10,17,18 . The extracellular domains of these mucins range from 500 to 5000 amino acids in length consisting largely of mucin tandem repeats 17,19 .…”

mentioning

confidence: 99%

Nanoarchitecture and dynamics of the mouse enteric glycocalyx examined by freeze-etching electron tomography and intravital microscopy

et al. 2020

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The glycocalyx is a highly hydrated, glycoprotein-rich coat shrouding many eukaryotic and prokaryotic cells. The intestinal epithelial glycocalyx, comprising glycosylated transmembrane mucins, is part of the primary host-microbe interface and is essential for nutrient absorption. Its disruption has been implicated in numerous gastrointestinal diseases. Yet, due to challenges in preserving and visualizing its native organization, glycocalyx structure-function relationships remain unclear. Here, we characterize the nanoarchitecture of the murine enteric glycocalyx using freeze-etching and electron tomography. Micrometer-long mucin filaments emerge from microvillar-tips and, through zigzagged lateral interactions form a three-dimensional columnar network with a 30 nm mesh. Filament-termini converge into globular structures~30 nm apart that are liquid-crystalline packed within a single plane. Finally, we assess glycocalyx deformability and porosity using intravital microscopy. We argue that the columnar network architecture and the liquid-crystalline packing of the filament termini allow the glycocalyx to function as a deformable size-exclusion filter of luminal contents.

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A Sweet Coating—How Bacteria Deal with Sugars

Cited by 14 publications

References 52 publications

Divergent Mechanisms of Interaction of Helicobacter pylori and Campylobacter jejuni with Mucus and Mucins

Divergent Mechanisms of Interaction of Helicobacter pylori and Campylobacter jejuni with Mucus and Mucins

Sweet-talk: role of host glycosylation in bacterial pathogenesis of the gastrointestinal tract

Nanoarchitecture and dynamics of the mouse enteric glycocalyx examined by freeze-etching electron tomography and intravital microscopy

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