ArticleScientific reports2015
Substitute sweeteners: diverse bacterial oligosaccharyltransferases with unique N-glycosylation site preferences.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 59 citations in OpenAlex.
- Topological reprogramming transforms an integral membrane oligosaccharyltransferase into a water-soluble glycosylation catalyst.bioRxiv : the preprint server for biology · 2026Article
- Glycoengineering strategies for constructing defined Mucin O-glycans.Frontiers in molecular biosciences · 2026Review
- Discovery of a single-subunit oligosaccharyltransferase that enables glycosylation of full-length IgG antibodies in bacteria.Nature communications · 2025Article
- Recent Advances in Bioconjugate Vaccine Development.Vaccines · 2025Review
- Glycosylation of Structured Protein Domains in Cell-Free Reaction Environments.ACS synthetic biology · 2025Article
- Recent Progress in Developing Extracellular Vesicles as Nanovehicles to Deliver Carbohydrate-Based Therapeutics and Vaccines.Vaccines · 2025Review
- Construction of anFrontiers in bioengineering and biotechnology · 2024Article
- Glycosylation Circuit Enables Improved Catalytic Properties for Recombinant Alkaline Phosphatase.ACS omega · 2023Article
- Rapid biosynthesis of glycoprotein therapeutics and vaccines from freeze-dried bacterial cell lysates.Nature protocols · 2023Review
- Progress towards a glycoconjugate vaccine against Group A Streptococcus.NPJ vaccines · 2023Review
- Ribosome Stalling ofACS synthetic biology · 2022Article
- Engineering a suite of E. coli strains for enhanced expression of bacterial polysaccharides and glycoconjugate vaccines.Microbial cell factories · 2022Article
- On-demand biomanufacturing of protective conjugate vaccines.Science advances · 2021Article
- Interplay of Carbohydrate and Carrier in Antibacterial Glycoconjugate Vaccines.Advances in biochemical engineering/biotechnology · 2021Article
- Glycosylation-on-a-Chip: A Flow-Based Microfluidic System for Cell-Free Glycoprotein Biosynthesis.Frontiers in molecular biosciences · 2021Article
- Bacterial Glycoengineering as a Biosynthetic Route to Customized Glycomolecules.Advances in biochemical engineering/biotechnology · 2021Article
- Cell-free systems for accelerating glycoprotein expression and biomanufacturing.Journal of industrial microbiology & biotechnology · 2020Review
- Synthetic Glycobiology: Parts, Systems, and Applications.ACS synthetic biology · 2020Review
- Cell-Free Synthetic Glycobiology: Designing and Engineering Glycomolecules Outside of Living Cells.Frontiers in chemistry · 2020Review
- Recent advances in the production of recombinant glycoconjugate vaccines.NPJ vaccines · 2019Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
The central enzyme in the Campylobacter jejuni asparagine-linked glycosylation pathway is the oligosaccharyltransferase (OST), PglB, which transfers preassembled glycans to specific asparagine residues in target proteins. While C. jejuni PglB (CjPglB) can transfer many diverse glycan structures, the acceptor sites that it recognizes are restricted predominantly to those having a negatively charged residue in the -2 position relative to the asparagine. Here, we investigated the acceptor-site preferences for 23 homologs with natural sequence variation compared to CjPglB. Using an ectopic trans-complementation assay for CjPglB function in glycosylation-competent Escherichia coli, we demonstrated in vivo activity for 16 of the candidate OSTs. Interestingly, the OSTs from Campylobacter coli, Campylobacter upsaliensis, Desulfovibrio desulfuricans, Desulfovibrio gigas, and Desulfovibrio vulgaris, exhibited significantly relaxed specificity towards the -2 position compared to CjPglB. These enzymes glycosylated minimal N-X-T motifs in multiple targets and each followed unique, as yet unknown, rules governing acceptor-site preferences. One notable example is D. gigas PglB, which was the only bacterial OST to glycosylate the Fc domain of human immunoglobulin G at its native 'QYNST' sequon. Overall, we find that a subset of bacterial OSTs follow their own rules for acceptor-site specificity, thereby expanding the glycoengineering toolbox with previously unavailable biocatalytic diversity.
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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.