ArticleJournal of bacteriology2006
Separate pathways for O acetylation of polymeric and monomeric sialic acids and identification of sialyl O-acetyl esterase in Escherichia coli K1.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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.
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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.
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Who cites it
34 citing papers in PubMed, 59 citations in OpenAlex.
- Advances in bacterial synthesis pathways of bioflocculants and their applications in mine wastewater treatment.World journal of microbiology & biotechnology · 2026Review
- A novel esterase regulates Klebsiella pneumoniae hypermucoviscosity and virulence.PLoS pathogens · 2024Article
- Biological functions of sialic acid as a component of bacterial endotoxin.Frontiers in microbiology · 2022Review
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- Article
- Sialic acid O-acetylation: From biosynthesis to roles in health and disease.The Journal of biological chemistry · 2021Review
- Structural and Biosynthetic Diversity of Nonulosonic Acids (NulOs) That Decorate Surface Structures in Bacteria.Trends in microbiology · 2021Review
- Pasteurella multocida: Genotypes and Genomics.Microbiology and molecular biology reviews : MMBR · 2019Review
- Genome-Wide Identification by Transposon Insertion Sequencing of Escherichia coli K1 Genes Essential forJournal of bacteriology · 2018Article
- The sialateThe Journal of biological chemistry · 2017Article
- Unexpected Diversity of Escherichia coli Sialate O-Acetyl Esterase NanS.Journal of bacteriology · 2016Article
- Discovery and characterization of de novo sialic acid biosynthesis in the phylum Fusobacterium.Glycobiology · 2016Article
- Detection of K1 antigen of Escherichia coli rods isolated from pregnant women and neonates.Folia microbiologica · 2014Article
- The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014Review
- Sialylation of outer membrane porin protein D: a mechanistic basis of antibiotic uptake in Pseudomonas aeruginosa.Molecular & cellular proteomics : MCP · 2014Article
- Control of the Escherichia coli sialoregulon by transcriptional repressor NanR.Journal of bacteriology · 2013Article
- Unified theory of bacterial sialometabolism: how and why bacteria metabolize host sialic acids.ISRN microbiology · 2013Article
- Chromatographic analysis of the Escherichia coli polysialic acid capsule.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Sialic acid metabolism and sialyltransferases: natural functions and applications.Applied microbiology and biotechnology · 2012Review
- Specific synthesis of neurostatin and gangliosides O-acetylated in the outer sialic acids using a sialate transferase.PloS one · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
O acetylation at carbon positions 7 or 9 of the sialic acid residues in the polysialic acid capsule of Escherichia coli K1 is catalyzed by a phase-variable contingency locus, neuO, carried by the K1-specific prophage, CUS-3. Here we describe a novel method for analyzing polymeric sialic acid O acetylation that involves the release of surface sialic acids by endo-N-acetylneuraminidase digestion, followed by fluorescent labeling and detection of quinoxalinone derivatives by chromatography. The results indicated that NeuO is responsible for the majority of capsule modification that takes place in vivo. However, a minor neuO-independent O acetylation pathway was detected that is dependent on the bifunctional polypeptide encoded by neuD. This pathway involves O acetylation of monomeric sialic acid and is regulated by another bifunctional enzyme, NeuA, which includes N-terminal synthetase and C-terminal sialyl O-esterase domains. A homologue of the NeuA C-terminal domain (Pm1710) in Pasteurella multocida was also shown to be an esterase, suggesting that it functions in the catabolism of acetylated environmental sialic acids. Our combined results indicate a previously unexpected complexity in the synthesis and catabolism of microbial sialic and polysialic acids. These findings are key to understanding the biological functions of modified sialic acids in E. coli K1 and other species and may provide new targets for drug or vaccine development.
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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.