ArticleThe Journal of biological chemistry2009
A new sialidase mechanism: bacteriophage K1F endo-sialidase is an inverting glycosidase.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 46 citations in OpenAlex.
- Mapping structural constraints and adaptive potential in a capsule-degrading phage tailspike protein.Science advances · 2026Article
- In planta engineering of polysialylated glycoproteins using salmonid polysialyltransferases.Scientific reports · 2026Article
- Polysialic acid is associated with immune activation in human peripheral blood nuclear cells.Glycobiology · 2026Article
- Mapping Structural Constraints and Adaptive Potential in a Capsule-Degrading Phage Tailspike Protein.bioRxiv : the preprint server for biology · 2025Article
- Targeting Pseudomonas aeruginosa biofilm with an evolutionary trained bacteriophage cocktail exploiting phage resistance trade-offs.Nature communications · 2024Article
- Site-specific immobilization of the endosialidase reveals QSOX2 is a novel polysialylated protein.Glycobiology · 2024Article
- Sialidase Inhibitors with Different Mechanisms.Journal of medicinal chemistry · 2022Review
- Crystal structure of the Propionibacterium acnes surface sialidase, a drug target for P. acnes-associated diseases.Glycobiology · 2022Article
- Review
- 7-Fluorosialyl Glycosides Are Hydrolysis Resistant but Readily Assembled by Sialyltransferases Providing Easy Access to More Metabolically Stable Glycoproteins.ACS central science · 2021Article
- Novel Drexlerviridae bacteriophage KMI8 with specific lytic activity against Klebsiella michiganensis and its biofilms.PloS one · 2021Article
- Sialidase substrates for Sialdiase assays - activity, specificity, quantification and inhibition.Glycoconjugate journal · 2020Review
- Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action.Nature communications · 2019Article
- Functional metagenomics identifies an exosialidase with an inverting catalytic mechanism that defines a new glycoside hydrolase family (GH156).The Journal of biological chemistry · 2018Article
- Conserved glycolipid termini in capsular polysaccharides synthesized by ATP-binding cassette transporter-dependent pathways in Gram-negative pathogens.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Decreasing the sialidase activity of multifunctional Pasteurella multocida α2-3-sialyltransferase 1 (PmST1) by site-directed mutagenesis.Molecular bioSystems · 2011Article
- Characterization of a ViI-like phage specific to Escherichia coli O157:H7.Virology journal · 2011Article
- Glycosidase inhibition: assessing mimicry of the transition state.Organic & biomolecular chemistry · 2010Review
- Functional viral metagenomics and the next generation of molecular tools.Trends in microbiology · 2010Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteriophages specific for Escherichia coli K1 express a tailspike protein that degrades the polysialic acid coat of E. coli K1 that is essential for bacteriophage infection. This enzyme is specific for polysialic acid and is a member of a family of endo-sialidases. This family is unusual because all other previously reported sialidases outside of this family are exo- or trans-sialidases. The recently determined structure of an endo-sialidase derived from bacteriophage K1F (endoNF) revealed an active site that lacks a number of the residues that are conserved in other sialidases, implying a new, endo-sialidase-specific catalytic mechanism. Using synthetic trifluoromethylumbelliferyl oligosialoside substrates, kinetic parameters for hydrolysis at a single cleavage site were determined. Measurement of kcat/Km at a series of pH values revealed a dependence on a single protonated group of pKa 5. Mutation of a putative active site acidic residue, E581A, resulted in complete loss of sialidase activity. Direct 1H NMR analysis of the hydrolysis of trifluoromethylumbelliferyl sialotrioside revealed that endoNF is an inverting sialidase. All other wild type sialidases previously reported are retaining glycosidases, implying a new mechanism of sialidase action specific to this family of endo-sialidases.
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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.