ArticlePloS one2012
Carbohydrate recognition by an architecturally complex α-N-acetylglucosaminidase from Clostridium perfringens.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
27 citing papers in PubMed, 55 citations in OpenAlex.
- Metatranscriptomic Analysis Reveals Functional Features of the Gastrointestinal Microbiota in Tibetan Pigs.Animals : an open access journal from MDPI · 2026Article
- Gatekeeping Dietary Fiber: The Role of Carbohydrate-Binding Modules in the Human Gut.Journal of microbiology and biotechnology · 2026Review
- Efficient mucin O-glycan degradation by specific mucin degrading intestinal bacteria: towards understanding enzyme-glycan interactions.Glycobiology · 2026Article
- Mucinase fromFrontiers in microbiology · 2026Article
- Pathogenic piscine intestinal coccidia infection alters gut microbiome in juvenile Asian seabass (Lates calcarifer).BMC veterinary research · 2025Article
- A Bacteroides thetaiotaomicron genetic locus encodes activities consistent with mucin O-glycoprotein processing and N-acetylgalactosamine metabolism.Nature communications · 2025Article
- Clostridium perfringens chitinases, key enzymes during early stages of necrotic enteritis in broiler chickens.PLoS pathogens · 2024Article
- Identifying the molecular basis of Laminin N-terminal domain CaBiophysical journal · 2024Article
- Structural and functional characterization of a multi-domain GH92 α-1,2-mannosidase from Neobacillus novalis.Acta crystallographica. Section D, Structural biology · 2023Article
- Qualitative and Quantitative Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Necrotic Enteritis in Broiler Chickens: A Review on the Pathogen, Pathogenesis, and Prevention.Microorganisms · 2022Review
- Effects of challenge withFrontiers in microbiology · 2022Article
- Architecturally complexProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Coccidia-Microbiota Interactions and Their Effects on the Host.Frontiers in cellular and infection microbiology · 2021Review
- Probiotic Bacillus amyloliquefaciens H57 ameliorates subclinical necrotic enteritis in broiler chicks by maintaining intestinal mucosal integrity and improving feed efficiency.Poultry science · 2020Article
- Trefoil factors share a lectin activity that defines their role in mucus.Nature communications · 2020Article
- Preliminary studies on development of a novel subunit vaccine targeting Clostridium perfringens mucolytic enzymes for the control of necrotic enteritis in broilers.Poultry science · 2019Article
- Functional and Structural Studies of a Multidomain Alginate Lyase from Persicobacter sp. CCB-QB2.Scientific reports · 2017Article
- Rethinking the role of alpha toxin in Clostridium perfringens-associated enteric diseases: a review on bovine necro-haemorrhagic enteritis.Veterinary research · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
Abstract
CpGH89 is a large multimodular enzyme produced by the human and animal pathogen Clostridium perfringens. The catalytic activity of this exo-α-D-N-acetylglucosaminidase is directed towards a rare carbohydrate motif, N-acetyl-β-D-glucosamine-α-1,4-D-galactose, which is displayed on the class III mucins deep within the gastric mucosa. In addition to the family 89 glycoside hydrolase catalytic module this enzyme has six modules that share sequence similarity to the family 32 carbohydrate-binding modules (CBM32s), suggesting the enzyme has considerable capacity to adhere to carbohydrates. Here we suggest that two of the modules, CBM32-1 and CBM32-6, are not functional as carbohydrate-binding modules (CBMs) and demonstrate that three of the CBMs, CBM32-3, CBM32-4, and CBM32-5, are indeed capable of binding carbohydrates. CBM32-3 and CBM32-4 have a novel binding specificity for N-acetyl-β-D-glucosamine-α-1,4-D-galactose, which thus complements the specificity of the catalytic module. The X-ray crystal structure of CBM32-4 in complex with this disaccharide reveals a mode of recognition that is based primarily on accommodation of the unique bent shape of this sugar. In contrast, as revealed by a series of X-ray crystal structures and quantitative binding studies, CBM32-5 displays the structural and functional features of galactose binding that is commonly associated with CBM family 32. The functional CBM32s that CpGH89 contains suggest the possibility for multivalent binding events and the partitioning of this enzyme to highly specific regions within the gastrointestinal tract.
Indexed as
Identifiers
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.