ArticleOpen biology2015
Increased efficiency of Campylobacter jejuni N-oligosaccharyltransferase PglB by structure-guided engineering.
Article in Open biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 70 citations in OpenAlex.
- Development and evaluation of a dual-target glycoconjugate againstFrontiers in immunology · 2026Article
- Characterizing and engineering post-translational modifications with high-throughput cell-free expression.Nature communications · 2025Article
- Investigation into the efficiency of diverse N-linking oligosaccharyltransferases for glycoengineering using a standardised cell-free assay.Microbial biotechnology · 2024Article
- Efficient Production of Self-Assembled Bioconjugate Nanovaccines againstNanomaterials (Basel, Switzerland) · 2024Article
- Progress towards a glycoconjugate vaccine against Group A Streptococcus.NPJ vaccines · 2023Review
- Engineering a suite of E. coli strains for enhanced expression of bacterial polysaccharides and glycoconjugate vaccines.Microbial cell factories · 2022Article
- Production of Vaccines Using Biological Conjugation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Genetic and process engineering strategies for enhanced recombinant N-glycoprotein production in bacteria.Microbial cell factories · 2021Article
- Resources and Methods for Engineering "Designer" Glycan-Binding Proteins.Molecules (Basel, Switzerland) · 2021Review
- Immunobiology of Carbohydrates: Implications for Novel Vaccine and Adjuvant Design Against Infectious Diseases.Frontiers in cellular and infection microbiology · 2021Review
- Bacterial Glycoengineering as a Biosynthetic Route to Customized Glycomolecules.Advances in biochemical engineering/biotechnology · 2021Article
- Interplay of Carbohydrate and Carrier in Antibacterial Glycoconjugate Vaccines.Advances in biochemical engineering/biotechnology · 2021Article
- Cell-free systems for accelerating glycoprotein expression and biomanufacturing.Journal of industrial microbiology & biotechnology · 2020Review
- Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies.Nature communications · 2019Article
- Glycoengineering bioconjugate vaccines, therapeutics, and diagnostics in E. coli.Glycobiology · 2019Review
- Harnessing glycoenzyme engineering for synthesis of bioactive oligosaccharides.Interface focus · 2019Review
- A platform for glycoengineering a polyvalent pneumococcal bioconjugate vaccine using E. coli as a host.Nature communications · 2019Article
- Recent advances in the production of recombinant glycoconjugate vaccines.NPJ vaccines · 2019Review
- Structure of bacterial oligosaccharyltransferase PglB bound to a reactive LLO and an inhibitory peptide.Scientific reports · 2018Article
- Chemoenzymatic Methods for the Synthesis of Glycoproteins.Chemical reviews · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conjugate vaccines belong to the most efficient preventive measures against life-threatening bacterial infections. Functional expression of N-oligosaccharyltransferase (N-OST) PglB of Campylobacter jejuni in Escherichia coli enables a simplified production of glycoconjugate vaccines in prokaryotic cells. Polysaccharide antigens of pathogenic bacteria can be covalently coupled to immunogenic acceptor proteins bearing engineered glycosylation sites. Transfer efficiency of PglBCj is low for certain heterologous polysaccharide substrates. In this study, we increased glycosylation rates for Salmonella enterica sv. Typhimurium LT2 O antigen (which lacks N-acetyl sugars) and Staphylococcus aureus CP5 polysaccharides by structure-guided engineering of PglB. A three-dimensional homology model of membrane-associated PglBCj, docked to the natural C. jejuni N-glycan attached to the acceptor peptide, was used to identify potential sugar-interacting residues as targets for mutagenesis. Saturation mutagenesis of an active site residue yielded the enhancing mutation N311V, which facilitated fivefold to 11-fold increased in vivo glycosylation rates as determined by glycoprotein-specific ELISA. Further rounds of in vitro evolution led to a triple mutant S80R-Q287P-N311V enabling a yield improvement of S. enterica LT2 glycoconjugates by a factor of 16. Our results demonstrate that bacterial N-OST can be tailored to specific polysaccharide substrates by structure-guided protein engineering.
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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.