ArticleThe Journal of biological chemistry2015
Streptococcus pneumoniae NanC: STRUCTURAL INSIGHTS INTO THE SPECIFICITY AND MECHANISM OF A SIALIDASE THAT PRODUCES A SIALIDASE INHIBITOR.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 46 citations in OpenAlex.
- Structural studies and functional engineering of NanX: an anhydro-sialic acid transporter from Escherichia coli.FEBS open bio · 2026Article
- Bacterial exo-α-sialidases subvert the complement system through desialylation.bioRxiv : the preprint server for biology · 2026Article
- Identification ofJournal of proteome research · 2025Article
- Novel strategies for PEDV to interfere with host antiviral immunity through Caspase-1.Virulence · 2025Article
- Mutant glycosidases for labeling sialoglycans with high specificity and affinity.Nature communications · 2025Article
- Characterisation of anhydro-sialic acid transporters from mucosa-associated bacteria.Microbiology (Reading, England) · 2024Article
- Functional and structural analyses reveal that a dual domain sialidase protects bacteria from complement killing through desialylation of complement factors.PLoS pathogens · 2023Article
- Identification of Subunits for Novel Universal Vaccines against Three Predominant Serogroups and the Emerging O145 among Avian Pathogenic Escherichia coli by Pan-RV Pipeline.Applied and environmental microbiology · 2023Article
- Co-infection of the respiratory epithelium, scene of complex functional interactions between viral, bacterial, and human neuraminidases.Frontiers in microbiology · 2023Review
- Role ofFrontiers in cellular and infection microbiology · 2023Review
- Multiple evolutionary origins reflect the importance of sialic acid transporters in the colonization potential of bacterial pathogens and commensals.Microbial genomics · 2021Article
- The putative Escherichia coli dehydrogenase YjhC metabolises two dehydrated forms of N-acetylneuraminate produced by some sialidases.Bioscience reports · 2020Article
- Exploration of Binding Mechanism of a PotentialInternational journal of molecular sciences · 2020Article
- Elucidation of a sialic acid metabolism pathway in mucus-foraging Ruminococcus gnavus unravels mechanisms of bacterial adaptation to the gut.Nature microbiology · 2019Article
- Soluble klotho regulates TRPC6 calcium signalingFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- 9-Azido-9-deoxy-2,3-difluorosialic Acid as a Subnanomolar Inhibitor against Bacterial Sialidases.The Journal of organic chemistry · 2019Article
- Comparative studies of catalytic pathways for Streptococcus pneumoniae sialidases NanA, NanB and NanC.Scientific reports · 2019Article
- Role of Pneumococcal NanA Neuraminidase Activity in Peripheral Blood.Frontiers in cellular and infection microbiology · 2019Article
- Triazole-linked transition state analogs as selective inhibitors against V. cholerae sialidase.Bioorganic & medicinal chemistry · 2018Article
- Catalytic mechanism of type C sialidase from Streptococcus pneumoniae: from covalent intermediate to final product.Journal of molecular modeling · 2018Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Streptococcus pneumoniae is an important human pathogen that causes a range of disease states. Sialidases are important bacterial virulence factors. There are three pneumococcal sialidases: NanA, NanB, and NanC. NanC is an unusual sialidase in that its primary reaction product is 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en, also known as DANA), a nonspecific hydrolytic sialidase inhibitor. The production of Neu5Ac2en from α2-3-linked sialosides by the catalytic domain is confirmed within a crystal structure. A covalent complex with 3-fluoro-β-N-acetylneuraminic acid is also presented, suggesting a common mechanism with other sialidases up to the final step of product formation. A conformation change in an active site hydrophobic loop on ligand binding constricts the entrance to the active site. In addition, the distance between the catalytic acid/base (Asp-315) and the ligand anomeric carbon is unusually short. These features facilitate a novel sialidase reaction in which the final step of product formation is direct abstraction of the C3 proton by the active site aspartic acid, forming Neu5Ac2en. NanC also possesses a carbohydrate-binding module, which is shown to bind α2-3- and α2-6-linked sialosides, as well as N-acetylneuraminic acid, which is captured in the crystal structure following hydration of Neu5Ac2en by NanC. Overall, the pneumococcal sialidases show remarkable mechanistic diversity while maintaining a common structural scaffold.
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