Host sialoglycans and bacterial sialidases: a mucosal perspective

Lewis, Amanda L.; Lewis, Warren G.

doi:10.1111/j.1462-5822.2012.01807.x

Cited by 188 publications

(183 citation statements)

References 54 publications

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“…In recurrent aphthous stomatitis, the mucins lost the ability to induce NETs due to loss of sialyl Lewis X . Possibly bacterial sialidases produced by the oral flora 40 contribute to the loss of sialyl Lewis X in salival mucins in recurrent aphthous stomatitis. In contrast, sialyl Lewis X was present on salival mucins in Behçet disease.…”

Section: Discussionmentioning

confidence: 99%

A novel mechanism for NETosis provides antimicrobial defense at the oral mucosa

Mohanty

Sjögren

Kahn

et al. 2015

Blood

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Section: Discussionmentioning

confidence: 99%

A novel mechanism for NETosis provides antimicrobial defense at the oral mucosa

Mohanty

Sjögren

Kahn

et al. 2015

Blood

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“…79 These oligosaccharides remain undigested in neonates and infants, therefore the intestinal microvilli of neonates have increased sialic acid and N-acetylglucosamine residues leading to proliferation of gut microbiota. 80,81 Recently, Joseph et al 82 explained a plausible linkage between sialic acid metabolism and the pathogenicity of C. sakazakii as it is the only Cronobacter species possessing the nanAKT gene cluster encoding for sialic acid utilization.…”

Section: Enterotoxinmentioning

confidence: 99%

Insights into virulence factors determining the pathogenicity ofCronobacter sakazakii

2015

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“…Sialidases, also referred to as neuraminidases, are key enzymes for the catabolism of sialic acid-containing oligosaccharides (9,10). These enzymes are found in higher animals and a variety of microorganisms, including viruses, bacteria, and protozoa (11).…”

mentioning

confidence: 99%

The Sialidases of Clostridium perfringens Type D Strain CN3718 Differ in Their Properties and Sensitivities to Inhibitors

McClane

2014

Appl Environ Microbiol

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Clostridium perfringens causes histotoxic infections and diseases originating in animal or human intestines. A prolific toxin producer, this bacterium also produces numerous enzymes, including sialidases, that may facilitate infection. C. perfringens type D strain CN3718 carries genes encoding three sialidases, including two large secreted sialidases (named NanI and NanJ) and one small sialidase (named NanH) that has an intracellular location in log-phase cultures but is present in supernatants of death phase cultures. Using isogenic mutants of CN3718 that are capable of expressing only NanJ, NanI, or NanH, the current study characterized the properties and activities of each sialidase. The optimal temperature determined for NanJ or NanH enzymatic activity was 37°C or 43°C, respectively, while NanI activity increased until temperature reached 48°C. NanI activity was also the most resistant against higher temperatures. All three sialidases showed optimal activities at pH 5.5. Compared to NanJ or NanH, NanI contributed most to the sialidase activity in CN3718 culture supernatants, regardless of the substrate sialic acid linkage; NanI also released the most sialic acid from Caco-2 cells. Only NanI activity was enhanced by trypsin pretreatment and then only for substrates with an ␣-2,3-or ␣-2,6-sialic acid linkage. NanJ and NanI activities were more sensitive than NanH activity to two sialidase inhibitors (N-acetyl-2,3-dehydro-2-deoxyneuraminic acid and siastatin B). The activities of the three sialidases were affected differently by several metal ions. These results indicated that each C. perfringens sialidase has distinct properties, which may allow these enzymes to play different roles depending upon environmental conditions.

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Host sialoglycans and bacterial sialidases: a mucosal perspective

Cited by 188 publications

References 54 publications

A novel mechanism for NETosis provides antimicrobial defense at the oral mucosa

A novel mechanism for NETosis provides antimicrobial defense at the oral mucosa

Insights into virulence factors determining the pathogenicity ofCronobacter sakazakii

The Sialidases of Clostridium perfringens Type D Strain CN3718 Differ in Their Properties and Sensitivities to Inhibitors

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