ReviewBiochemical Society transactions2016
Sialidases from gut bacteria: a mini-review.
Review in Biochemical Society transactions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
97 citing papers in PubMed, 164 citations in OpenAlex.
- Sialidase inhibitor modulates gut microbiota and enhances mucosal protection in the treatment of ulcerative colitis.mSystems · 2026Trial
- Functional Heterogeneity of the Autism Spectrum Disorder-Associated Gut Microbial Ecosystem Revealed by Fecal Lipopolysaccharides and Bacterial Proteomic Profiling.Chembiochem : a European journal of chemical biology · 2026Article
- Innovative Approaches Against Planktonic and Biofilm-ProducingVeterinary sciences · 2026Review
- Defined O-acetylated Neu5Ac substrates reveal position-specific preferences of gut bacterial sialidases.Glycobiology · 2026Article
- Structural studies and functional engineering of NanX: an anhydro-sialic acid transporter from Escherichia coli.FEBS open bio · 2026Article
- Mucin Type Drives Composition and Mucin Glycan Degradation of an In Vitro Synthetic Microbial Community.Environmental microbiology · 2026Article
- Identification of Sialidase-Producing Bacteria in the Tsetse Gut and Characterisation of a Paenibacillus Sialidase: A Potential Tool for Paratransgenic Control of African Trypanosomes.Research square · 2026Article
- Bacterial exo-α-sialidases subvert the complement system through desialylation.bioRxiv : the preprint server for biology · 2026Article
- Efficient mucin O-glycan degradation by specific mucin degrading intestinal bacteria: towards understanding enzyme-glycan interactions.Glycobiology · 2026Article
- Draft genome assemblies of threemicroPublication biology · 2026Article
- A Viral Neuraminidase-Specific Sensor for Taste-Based Detection of Influenza.ACS central science · 2025Article
- Dysbiosis-associated gut bacteriumMicrobiology spectrum · 2025Article
- The cervical microbiome of ewe breeds with known divergent fertility following artificial insemination with frozen-thawed semen.Scientific reports · 2025Article
- Structural and functional insights into metal coordination and substrate recognition of Akkermansia muciniphila sialidase Amuc_1547.Molecular biomedicine · 2025Article
- Genomic insights into the beneficial potential ofMicrobial genomics · 2025Article
- Acute and Subacute Toxicity of Sialidase FromVeterinary medicine international · 2025Article
- Species-level verification ofmSystems · 2024Article
- The immune interactions of gut glycans and microbiota in health and disease.Molecular microbiology · 2024Review
- Glycosphingolipids: from metabolism to chemoenzymatic total synthesis.Organic & biomolecular chemistry · 2024Review
- Exploring the genomic traits of infant-associated microbiota members from a Zimbabwean cohort.BMC genomics · 2024Article
37 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Sialidases are a large group of enzymes, the majority of which catalyses the cleavage of terminal sialic acids from complex carbohydrates on glycoproteins or glycolipids. In the gastrointestinal (GI) tract, sialic acid residues are mostly found in terminal location of mucins via α2-3/6 glycosidic linkages. Many enteric commensal and pathogenic bacteria can utilize sialic acids as a nutrient source, but not all express the sialidases that are required to release free sialic acid. Sialidases encoded by gut bacteria vary in terms of their substrate specificity and their enzymatic reaction. Most are hydrolytic sialidases, which release free sialic acid from sialylated substrates. However, there are also examples with transglycosylation activities. Recently, a third class of sialidases, intramolecular trans-sialidase (IT-sialidase), has been discovered in gut microbiota, releasing (2,7-anhydro-Neu5Ac) 2,7-anydro-N-acetylneuraminic acid instead of sialic acid. Reaction specificity varies, with hydrolytic sialidases demonstrating broad activity against α2,3-, α2,6- and α2,8-linked substrates, whereas IT-sialidases tend to be specific for α2,3-linked substrates. In this mini-review, we summarize the current knowledge on the structural and biochemical properties of sialidases involved in the interaction between gut bacteria and epithelial surfaces.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.