Evidence map›Paper›PMID 21131519›Full record

ArticleApplied and environmental microbiology2011

Production of secretory and extracellular N-linked glycoproteins in Escherichia coli.

Adam C Fisher, Charles H Haitjema, Cassandra Guarino, Eda Çelik, Christine E Endicott, Craig A Reading, Judith H Merritt, A Celeste Ptak, Sheng Zhang, Matthew P DeLisa

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.7field-weighted citation impact, top 5% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

53 citing papers in PubMed, 137 citations in OpenAlex.

  1. Article
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  4. Review
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  10. Review
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  12. Ribosome Stalling ofACS synthetic biology · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Production of Vaccines Using Biological Conjugation.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  17. Article
  18. Shotgun scanning glycomutagenesis: A simple and efficient strategy for constructing and characterizing neoglycoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
  20. Bacterial Glycoengineering as a Biosynthetic Route to Customized Glycomolecules.Advances in biochemical engineering/biotechnology · 2021
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Adam C FisherGlycobia, Inc., 33 Thornwood Drive, Ithaca, New York 14850, USA.
Charles H Haitjema
Cassandra Guarino
Eda Çelik
Christine E Endicott
Craig A Reading
Judith H Merritt
A Celeste Ptak
Sheng Zhang
Matthew P DeLisa
Cornell University · USGlycobia (United States) · US

Funding

Glycophage arrays for the discovery of biomarkers in diseaseR43GM086965 · NIGMS · GLYCOBIA, INC. · PI FISHER, ADAM CHARLES · 2009 to 2009
$200k
Glycosylation of full-length antibodies in Escherichia coliR43GM087766 · NIGMS · GLYCOBIA, INC. · PI FISHER, ADAM CHARLES · 2009 to 2009
$82k
NIGMS NIH HHS R43 GM086965NIGMS NIH HHS R43 GM087766
6 · The paper itself

Abstract

The Campylobacter jejuni pgl gene cluster encodes a complete N-linked protein glycosylation pathway that can be functionally transferred into Escherichia coli. In this system, we analyzed the interplay between N-linked glycosylation, membrane translocation and folding of acceptor proteins in bacteria. We developed a recombinant N-glycan acceptor peptide tag that permits N-linked glycosylation of diverse recombinant proteins expressed in the periplasm of glycosylation-competent E. coli cells. With this "glycosylation tag," a clear difference was observed in the glycosylation patterns found on periplasmic proteins depending on their mode of inner membrane translocation (i.e., Sec, signal recognition particle [SRP], or twin-arginine translocation [Tat] export), indicating that the mode of protein export can influence N-glycosylation efficiency. We also established that engineered substrate proteins targeted to environments beyond the periplasm, such as the outer membrane, the membrane vesicles, and the extracellular medium, could serve as substrates for N-linked glycosylation. Taken together, our results demonstrate that the C. jejuni N-glycosylation machinery is compatible with distinct secretory mechanisms in E. coli, effectively expanding the N-linked glycome of recombinant E. coli. Moreover, this simple glycosylation tag strategy expands the glycoengineering toolbox and opens the door to bacterial synthesis of a wide array of recombinant glycoprotein conjugates.

Indexed as

Bacterial ProteinsCampylobacter jejuniCulture MediaEscherichia coliEscherichia coli ProteinsGlycoproteinsGlycosylationPeriplasmPolysaccharidesProtein EngineeringProtein TransportRecombinant ProteinsSignal Recognition ParticleBacterial ProteinsCulture MediaEscherichia coli ProteinsGlycoproteinsPolysaccharidesRecombinant ProteinsSignal Recognition Particle

Identifiers

PMID21131519
PMCPMC3028701
OpenAlexW2167215594

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.