ArticleBioorganic & medicinal chemistry2021
Exploring a combined Escherichia coli-based glycosylation and in vitro transglycosylation approach for expression of glycosylated interferon alpha.
Article in Bioorganic & medicinal chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- From Genetic Engineering to Preclinical Safety: A Study on Recombinant Human Interferons.International journal of molecular sciences · 2025Article
- Enhancing recombinant growth factor and serum protein production for cultivated meat manufacturing.Microbial cell factories · 2025Review
- Multiplex genetic manipulations in Clostridium butyricum and Clostridium sporogenes to secrete recombinant antigen proteins for oral-spore vaccination.Microbial cell factories · 2024Article
- Construction of anFrontiers in bioengineering and biotechnology · 2024Article
- Article
- Identification of the effect ofRSC advances · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The conventional use of E. coli system for protein expression is limited to non-glycosylated proteins. While yeast, insect and mammalian systems are available to produce heterologous glycoproteins, developing an engineered E. coli-based glycosylation platform will provide a faster, more economical, and more convenient alternative. In this work, we present a two-step approach for production of a homogeneously glycosylated eukaryotic protein using the E. coli expression system. Human interferon α-2b (IFNα) is used as a model protein to illustrate this glycosylation scheme. In the first step, the N-glycosyltransferase from Actinobacillus pleuropneumoniae (ApNGT) is co-expressed for in vivo transfer of a glucose residue to IFNα at an NX(S/T) N-glycosylation sequon. Several E. coli systems were examined to evaluate the efficiency of IFNα N-glucosylation. In the second step, the N-glucosylated protein is efficiently elaborated with biantennary sialylated complex-type N-glycan using an in vitro chemoenzymatic method. The N-glycosylated IFNα product was found to be biologically active and displayed significantly improved proteolytic stability. This work presents a feasible E. coli-based glycosylation machinery for producing therapeutic eukaryotic glycoproteins.
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