ArticleScientific reports2017
X-ray crystallographic structure of a bacterial polysialyltransferase provides insight into the biosynthesis of capsular polysialic acid.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 19 citations in OpenAlex.
- Chemoenzymatic Synthesis of Well-Defined α(2,8)- and α(2,9)-Linked Oligosialosides.Angewandte Chemie (International ed. in English) · 2026Article
- Polysialic Acid Modulation of Glutamate Receptors and Synaptic Mechanisms Underlying Neuronal Plasticity.NeuroSci · 2026Review
- Identification of Polysialic Acid and Chondroitin-like Polysaccharides ofACS infectious diseases · 2026Article
- From duplication to fusion: Expanding Dayhoff's model of protein evolution.Protein science : a publication of the Protein Society · 2025Review
- Transition transferases prime bacterial capsule polymerization.Nature chemical biology · 2025Article
- Bacterial capsules: Occurrence, mechanism, and function.NPJ biofilms and microbiomes · 2024Review
- A multi-enzyme machine polymerizes the Haemophilus influenzae type b capsule.Nature chemical biology · 2023Article
- Sweet impersonators: Molecular mimicry of host glycans by bacteria.Glycobiology · 2022Review
- 3-Computational and structural biotechnology journal · 2022Article
- Processivity in Bacterial Glycosyltransferases.ACS chemical biology · 2020Review
- Super-Resolution Fluorescence Microscopy Study of the Production of K1 Capsules by Escherichia coli: Evidence for the Differential Distribution of the Capsule at the Poles and the Equator of the Cell.Langmuir : the ACS journal of surfaces and colloids · 2019Article
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10 authors at 3 institutions in 2 countries.
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Abstract
Polysialic acid (polySia) is a homopolymeric saccharide that is associated with some neuroinvasive pathogens and is found on selective cell types in their eukaryotic host. The presence of a polySia capsule on these bacterial pathogens helps with resistance to phagocytosis, cationic microbial peptides and bactericidal antibody production. The biosynthesis of bacterial polySia is catalysed by a single polysialyltransferase (PST) transferring sialic acid from a nucleotide-activated donor to a lipid-linked acceptor oligosaccharide. Here we present the X-ray structure of the bacterial PST from Mannheimia haemolytica serotype A2, thereby defining the architecture of this class of enzymes representing the GT38 family. The structure reveals a prominent electropositive groove between the two Rossmann-like domains forming the GT-B fold that is suitable for binding of polySia chain products. Complex structures of PST with a sugar donor analogue and an acceptor mimetic combined with kinetic studies of PST active site mutants provide insight into the principles of substrate binding and catalysis. Our results are the basis for a molecular understanding of polySia biosynthesis in bacteria and might assist the production of polysialylated therapeutic reagents and the development of novel antibiotics.
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