ArticleBioorganic & medicinal chemistry2013
A two-step enzymatic glycosylation of polypeptides with complex N-glycans.
Article in Bioorganic & medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 60 citations in OpenAlex.
- Article
- Exploring a combined Escherichia coli-based glycosylation and in vitro transglycosylation approach for expression of glycosylated interferon alpha.Bioorganic & medicinal chemistry · 2021Article
- Bacterial Glycoengineering as a Biosynthetic Route to Customized Glycomolecules.Advances in biochemical engineering/biotechnology · 2021Article
- Glycopeptide drugs: A pharmacological dimension between "Small Molecules" and "Biologics".Peptides · 2020Review
- Synthetic Glycobiology: Parts, Systems, and Applications.ACS synthetic biology · 2020Review
- On enzymatic remodeling of IgG glycosylation; unique tools with broad applications.Glycobiology · 2020Review
- Sequential Glycosylation of Proteins with Substrate-SpecificACS central science · 2020Article
- Homogeneous production and characterization of recombinant N-GlcNAc-protein in Pichia pastoris.Microbial cell factories · 2020Article
- A cell-free biosynthesis platform for modular construction of protein glycosylation pathways.Nature communications · 2019Article
- Chemoenzymatic Methods for the Synthesis of Glycoproteins.Chemical reviews · 2018Review
- Design of glycosylation sites by rapid synthesis and analysis of glycosyltransferases.Nature chemical biology · 2018Article
- Production of homogeneous glycoprotein with multisite modifications by an engineeredThe Journal of biological chemistry · 2017Article
- Sequential Double "Clicks" toward Structurally Well-Defined HeterogeneousAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2017Article
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- Optimal Synthetic Glycosylation of a Therapeutic Antibody.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2016Article
- Optimal Synthetic Glycosylation of a Therapeutic Antibody.Angewandte Chemie (International ed. in English) · 2016Article
- Hijacking bacterial glycosylation for the production of glycoconjugates, from vaccines to humanised glycoproteins.The Journal of pharmacy and pharmacology · 2015Review
- The HMW1C-like glycosyltransferases--an enzyme family with a sweet tooth for simple sugars.PLoS pathogens · 2014Article
- Molecular analysis of an alternative N-glycosylation machinery by functional transfer from Actinobacillus pleuropneumoniae to Escherichia coli.The Journal of biological chemistry · 2014Article
- Chemical and chemoenzymatic synthesis of glycoproteins for deciphering functions.Chemistry & biology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
A chemoenyzmatic method for direct glycosylation of polypeptides is described. The method consists of two site-specific enzymatic glycosylation steps: introduction of a glucose moiety at the consensus N-glycosylation sequence (NXS/T) in a polypeptide by an N-glycosyltransferase (NGT) and attachment of a complex N-glycan to the glucose primer by an endoglycosidase (ENGase)-catalyzed transglycosylation. Our experiments demonstrated that a relatively small excess of the UDP-Glc (the donor substrate) was sufficient for an effective glucosylation of polypeptides by the NGT, and different high-mannose and complex type N-glycans could be readily transferred to the glucose moiety by ENGases to provide full-size glycopeptides. The usefulness of the chemoenzymatic method was exemplified by an efficient synthesis of a complex glycoform of polypeptide C34, a potent HIV inhibitor derived from HIV-1 gp41. A comparative study indicated that the Glc-peptide was equally efficient as the natural GlcNAc-peptide to serve as an acceptor in the transglycosylation with sugar oxazoline as the donor substrate. Interestingly, the Glc-Asn linked glycopeptide was completely resistant to PNGase F digestion, in contrast to the GlcNAc-Asn linked natural glycopeptide that is an excellent substrate for hydrolysis. In addition, the Glc-Asn linked glycopeptide showed at least 10-fold lower hydrolytic activity toward Endo-M than the natural GlcNAc-Asn linked glycopeptide. The chemoenzymatic glycosylation method described here provides an efficient way to introducing complex N-glycans into polypeptides, for gain of novel properties that could be valuable for drug discovery.
Indexed as
Identifiers
What OpenQuestion holds
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.