ArticleThe Journal of biological chemistry2014
Molecular analysis of an alternative N-glycosylation machinery by functional transfer from Actinobacillus pleuropneumoniae to Escherichia coli.
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 36 papers.
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36 citing papers in PubMed, 82 citations in OpenAlex.
- RENBP inhibition amplifies metabolic glycan labeling efficiency of antigen-presenting cells in vitro and in vivo.Cell chemical biology · 2025Article
- Rational design of a highly activeEngineering microbiology · 2024Article
- Modulating antibody effector functions by Fc glycoengineering.Biotechnology advances · 2023Review
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- GlycoCAP: A Cell-Free, Bacterial Glycosylation Platform for Building Clickable Azido-Sialoglycoproteins.ACS synthetic biology · 2023Article
- Identification of the effect ofRSC advances · 2022Article
- Strategies for efficient production of recombinant proteins in Escherichia coli: alleviating the host burden and enhancing protein activity.Microbial cell factories · 2022Review
- 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
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
- Exploring a combined Escherichia coli-based glycosylation and in vitro transglycosylation approach for expression of glycosylated interferon alpha.Bioorganic & medicinal chemistry · 2021Article
- Semiprocessive Hyperglycosylation of Adhesin by Bacterial ProteinACS chemical biology · 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
- A cell-free biosynthesis platform for modular construction of protein glycosylation pathways.Nature communications · 2019Article
- Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies.Nature communications · 2019Article
- Glycoengineering bioconjugate vaccines, therapeutics, and diagnostics in E. coli.Glycobiology · 2019Review
- A survival selection strategy for engineering synthetic binding proteins that specifically recognize post-translationally phosphorylated proteins.Nature communications · 2019Article
- Cytoplasmic glycoengineering of Apx toxin fragments in the development of Actinobacillus pleuropneumoniae glycoconjugate vaccines.BMC veterinary research · 2019Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-Linked protein glycosylation is a frequent post-translational modification that can be found in all three domains of life. In a canonical, highly conserved pathway, an oligosaccharide is transferred by a membrane-bound oligosaccharyltransferase from a lipid donor to asparagines in the sequon NX(S/T) of secreted polypeptides. The δ-proteobacterium Actinobacillus pleuropneumoniae encodes an unusual pathway for N-linked protein glycosylation. This pathway takes place in the cytoplasm and is mediated by a soluble N-glycosyltransferase (NGT) that uses nucleotide-activated monosaccharides to glycosylate asparagine residues. To characterize the process of cytoplasmic N-glycosylation in more detail, we studied the glycosylation in A. pleuropneumoniae and functionally transferred the glycosylation system to Escherichia coli. N-Linked glucose specific human sera were used for the analysis of the glycosylation process. We identified autotransporter adhesins as the preferred protein substrate of NGT in vivo, and in depth analysis of the modified sites in E. coli revealed a surprisingly relaxed peptide substrate specificity. Although NX(S/T) is the preferred acceptor sequon, we detected glycosylation of alternative sequons, including modification of glutamine and serine residues. We also demonstrate the use of NGT to glycosylate heterologous proteins. Therefore, our study could provide the basis for a novel route for the engineering of N-glycoproteins in bacteria.
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