ArticleMolecular microbiology2007
Biochemical characterization of a Neisseria meningitidis polysialyltransferase reveals novel functional motifs in bacterial sialyltransferases.
Article in Molecular microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 83 citations in OpenAlex.
- Investigation of bioluminescence-based assays for determination of kinetic parameters for the bifunctional Neisseria meningitidis serogroup W capsule polymerase.BMC research notes · 2021Article
- Review
- Semiprocessive Hyperglycosylation of Adhesin by Bacterial ProteinACS chemical biology · 2021Article
- ThemBio · 2020Article
- Processivity in Bacterial Glycosyltransferases.ACS chemical biology · 2020Review
- Nonulosonic acids contribute to the pathogenicity of the oral bacteriumInterface focus · 2019Review
- Determination of the binding affinities of Neisseria meningitidis serogroup W capsule polymerase with two nucleotide sugar substrates.BMC research notes · 2018Article
- Article
- Review
- Reconstruction of the sialylation pathway in the ancestor of eukaryotes.Scientific reports · 2018Article
- Efficient solid-phase synthesis of meningococcal capsular oligosaccharides enables simple and fast chemoenzymatic vaccine production.The Journal of biological chemistry · 2018Article
- Haemophilus parasuis α-2,3-sialyltransferase-mediated lipooligosaccharide sialylation contributes to bacterial pathogenicity.Virulence · 2018Article
- X-ray crystallographic structure of a bacterial polysialyltransferase provides insight into the biosynthesis of capsular polysialic acid.Scientific reports · 2017Article
- Article
- Paired Siglec receptors generate opposite inflammatory responses to a human-specific pathogen.The EMBO journal · 2017Article
- Polysialic acid sustains cancer cell survival and migratory capacity in a hypoxic environment.Scientific reports · 2016Article
- Regulation of capsule in Neisseria meningitidis.Critical reviews in microbiology · 2016Review
- Genetic and Molecular Basis of Kingella kingae Encapsulation.Infection and immunity · 2016Article
- Bacterial β-Kdo glycosyltransferases represent a new glycosyltransferase family (GT99).Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Identification and Biochemical Characterization of the Novel α2,3-Sialyltransferase WbwA from Pathogenic Escherichia coli Serotype O104.Journal of bacteriology · 2015Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The extracellular polysaccharide capsule is an essential virulence factor of Neisseria meningitidis, a leading cause of severe bacterial meningitis and sepsis. Serogroup B strains, the primary disease causing isolates in Europe and America, are encapsulated in alpha-2,8 polysialic acid (polySia). The capsular polymer is synthesized from activated sialic acid by action of a membrane-associated polysialyltransferase (NmB-polyST). Here we present a comprehensive characterization of NmB-polyST. Different from earlier studies, we show that membrane association is not essential for enzyme functionality. Recombinant NmB-polyST was expressed, purified and shown to synthesize long polySia chains in a non-processive manner in vitro. Subsequent structure-function analyses of NmB-polyST based on refined sequence alignments allowed the identification of two functional motifs in bacterial sialyltransferases. Both (D/E-D/E-G and HP motif) are highly conserved among different sialyltransferase families with otherwise little or no sequence identity. Their functional importance for enzyme catalysis and CMP-Neu5Ac binding was demonstrated by mutational analysis of NmB-polyST and is emphasized by structural data available for the Pasteurella multocida sialyltransferase PmST1. Together our data are the first description of conserved functional elements in the highly diverse families of bacterial (poly)sialyltransferases and thus provide an advanced basis for understanding structure-function relations and for phylogenetic sorting of these important enzymes.
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