ArticleThe Journal of biological chemistry2013
Biochemical and biophysical characterization of the sialyl-/hexosyltransferase synthesizing the meningococcal serogroup W135 heteropolysaccharide capsule.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
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- 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
- A Chemoenzymatic Synthon Strategy for SynthesizingThe Journal of organic chemistry · 2020Article
- Size-Controlled Chemoenzymatic Synthesis of Homogeneous Oligosaccharides ofACS catalysis · 2020Article
- Determination of the binding affinities of Neisseria meningitidis serogroup W capsule polymerase with two nucleotide sugar substrates.BMC research notes · 2018Article
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- 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
- New Helical Binding Domain Mediates a Glycosyltransferase Activity of a Bifunctional Protein.The Journal of biological chemistry · 2016Article
- 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
- 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
- Dissection of hexosyl- and sialyltransferase domains in the bifunctional capsule polymerases from Neisseria meningitidis W and Y defines a new sialyltransferase family.The Journal of biological chemistry · 2014Article
- Molecular cloning and functional characterization of components of the capsule biosynthesis complex of Neisseria meningitidis serogroup A: toward in vitro vaccine production.The Journal of biological chemistry · 2014Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neisseria meningitidis (Nm) is a leading cause of bacterial meningitis and sepsis. Crucial virulence determinants of pathogenic Nm strains are the polysaccharide capsules that support invasion by hindering complement attack. In NmW-135 and NmY the capsules are built from the repeating units (→ 6)-α-D-Gal-(1 → 4)-α-Neu5Ac-(2 →)n and (→ 6)-α-D-Glc-(1 → 4)-α-Neu5Ac-(2 →)n, respectively. These unusual heteropolymers represent unique examples of a conjugation between sialic acid and hexosyl-sugars in a polymer chain. Moreover, despite the various catalytic strategies needed for sialic acid and hexose transfer, single enzymes (SiaDW-135/Y) have been identified to form these heteropolymers. Here we used SiaDW-135 as a model system to delineate structure-function relationships. In size exclusion chromatography active SiaDW-135 migrated as a monomer. Fold recognition programs suggested two separate glycosyltransferase domains, both containing a GT-B-fold. Based on conserved motifs predicted folds could be classified as a hexosyl- and sialyltransferase. To analyze enzyme properties and interplay of the two identified glycosyltransferase domains, saturation transfer difference NMR and mutational studies were carried out. Simultaneous and independent binding of UDP-Gal and CMP-Sia was seen in the absence of an acceptor as well as when the catalytic cycle was allowed to proceed. Enzyme variants with only one functionality were generated by site-directed mutagenesis and shown to complement each other in trans when combined in an in vitro test system. Together the data strongly suggests that SiaDW-135 has evolved by fusion of two independent ancestral genes encoding sialyl- and galactosyltransferase activity.
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