ArticlePLoS neglected tropical diseases2015
Carbohydrate Recognition Specificity of Trans-sialidase Lectin Domain from Trypanosoma congolense.
Article in PLoS neglected tropical diseases, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- 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
- CLEC18A interacts with sulfated glycosaminoglycans and controls clear cell renal cell carcinoma progression.The FEBS journal · 2026Article
- Dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) is a cellular receptor for delta inulin adjuvant.Immunology and cell biology · 2024Article
- Novel insights into the host cell glycan binding profile of human metapneumovirus.Journal of virology · 2024Article
- Article
- Ucl fimbriae regulation and glycan receptor specificity contribute to gut colonisation by extra-intestinal pathogenic Escherichia coli.PLoS pathogens · 2022Article
- Cooperativity of catalytic and lectin-like domain of Trypanosoma congolense trans-sialidase modulates its catalytic activity.PLoS neglected tropical diseases · 2022Article
- Article
- The cell surface protein MUL_3720 confers binding of the skin pathogen Mycobacterium ulcerans to sulfated glycans and keratin.PLoS neglected tropical diseases · 2021Article
- The Role of Glycosylation in Infectious Diseases.Advances in experimental medicine and biology · 2021Review
- Article
- All major cholesterol-dependent cytolysins use glycans as cellular receptors.Science advances · 2020Article
- Solution structure, glycan specificity and of phenol oxidase inhibitory activity of Anopheles C-type lectins CTL4 and CTLMA2.Scientific reports · 2019Article
- Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin.Nature communications · 2019Article
- Enhancing vector refractoriness to trypanosome infection: achievements, challenges and perspectives.BMC microbiology · 2018Article
- The HMW2 adhesin of non-typeable Haemophilus influenzae is a human-adapted lectin that mediates high-affinity binding to 2-6 linked N-acetylneuraminic acid glycans.Biochemical and biophysical research communications · 2018Article
- Glycointeractions in bacterial pathogenesis.Nature reviews. Microbiology · 2018Review
- The Bexsero Neisseria meningitidis serogroup B vaccine antigen NHBA is a high-affinity chondroitin sulfate binding protein.Scientific reports · 2018Article
- Lectin activity of the pneumococcal pilin proteins.Scientific reports · 2017Article
- The glycointeractome of serogroup B Neisseria meningitidis strain MC58.Scientific reports · 2017Article
Corrections and comments
- Erratum issued
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fourteen different active Trypanosoma congolense trans-sialidases (TconTS), 11 variants of TconTS1 besides TconTS2, TconTS3 and TconTS4, have been described. Notably, the specific transfer and sialidase activities of these TconTS differ by orders of magnitude. Surprisingly, phylogenetic analysis of the catalytic domains (CD) grouped each of the highly active TconTS together with the less active enzymes. In contrast, when aligning lectin-like domains (LD), the highly active TconTS grouped together, leading to the hypothesis that the LD of TconTS modulates its enzymatic activity. So far, little is known about the function and ligand specificity of these LDs. To explore their carbohydrate-binding potential, glycan array analysis was performed on the LD of TconTS1, TconTS2, TconTS3 and TconTS4. In addition, Saturation Transfer Difference (STD) NMR experiments were done on TconTS2-LD for a more detailed analysis of its lectin activity. Several mannose-containing oligosaccharides, such as mannobiose, mannotriose and higher mannosylated glycans, as well as Gal, GalNAc and LacNAc containing oligosaccharides were confirmed as binding partners of TconTS1-LD and TconTS2-LD. Interestingly, terminal mannose residues are not acceptor substrates for TconTS activity. This indicates a different, yet unknown biological function for TconTS-LD, including specific interactions with oligomannose-containing glycans on glycoproteins and GPI anchors found on the surface of the parasite, including the TconTS itself. Experimental evidence for such a scenario is presented.
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