ArticleThe Journal of biological chemistry2014
Dissection of hexosyl- and sialyltransferase domains in the bifunctional capsule polymerases from Neisseria meningitidis W and Y defines a new sialyltransferase family.
Article in The Journal of biological chemistry, 2014. 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, 31 citations in OpenAlex.
- Transition transferases prime bacterial capsule polymerization.Nature chemical biology · 2025Article
- Glycosphingolipids: from metabolism to chemoenzymatic total synthesis.Organic & biomolecular chemistry · 2024Review
- Towards Computationally Guided Design and Engineering of aProcesses (Basel, Switzerland) · 2021Article
- Investigation of bioluminescence-based assays for determination of kinetic parameters for the bifunctional Neisseria meningitidis serogroup W capsule polymerase.BMC research notes · 2021Article
- Recent and Future Advances in the Chemoenzymatic Synthesis of Homogeneous Glycans for Bacterial Glycoconjugate Vaccine Development.Vaccines · 2021Review
- Size-Controlled Chemoenzymatic Synthesis of Homogeneous Oligosaccharides ofACS catalysis · 2020Article
- Whole-Genome Sequencing for Characterization of Capsule Locus and Prediction of Serogroup of Invasive Meningococcal Isolates.Journal of clinical microbiology · 2019Article
- 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
- Identification and biochemical characterization of WbwB, a novel UDP-Gal: Neu5Ac-R α1,4-galactosyltransferase from the intestinal pathogen Escherichia coli serotype O104.Glycoconjugate journal · 2018Article
- Efficient solid-phase synthesis of meningococcal capsular oligosaccharides enables simple and fast chemoenzymatic vaccine production.The Journal of biological chemistry · 2018Article
- Single polysaccharide assembly protein that integrates polymerization, termination, and chain-length quality control.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Regulation of capsule in Neisseria meningitidis.Critical reviews in microbiology · 2016Review
- Genomic Investigation Reveals Highly Conserved, Mosaic, Recombination Events Associated with Capsular Switching among Invasive Neisseria meningitidis Serogroup W Sequence Type (ST)-11 Strains.Genome biology and evolution · 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
- An efficient cell free enzyme-based total synthesis of a meningococcal vaccine candidate.NPJ vaccines · 2016Article
- The capsule polymerase CslB of Neisseria meningitidis serogroup L catalyzes the synthesis of a complex trimeric repeating unit comprising glycosidic and phosphodiester linkages.The Journal of biological chemistry · 2015Article
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Crucial virulence determinants of disease causing Neisseria meningitidis species are their extracellular polysaccharide capsules. In the serogroups W and Y, these are heteropolymers of the repeating units (→6)-α-d-Gal-(1→4)-α-Neu5Ac-(2→)n in NmW and (→6)-α-d-Glc-(1→4)-α-Neu5Ac-(2→)n in NmY. The capsule polymerases, SiaDW and SiaDY, which synthesize these highly unusual polymers, are composed of two predicted GT-B fold domains separated by a large stretch of amino acids (aa 399-762). We recently showed that residues critical to the hexosyl- and sialyltransferase activity are found in the predicted N-terminal (aa 1-398) and C-terminal (aa 763-1037) GT-B fold domains, respectively. Here we use a mutational approach and synthetic fluorescent substrates to define the boundaries of the hexosyl- and sialyltransferase domains. Our results reveal that the active sialyltransferase domain extends well beyond the predicted C-terminal GT-B domain and defines a new glycosyltransferase family, GT97, in CAZy (Carbohydrate-Active enZYmes Database).
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