Evidence map›Paper›PMID 18296643›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Engineering of mucin-type human glycoproteins in yeast cells.

Koh Amano, Yasunori Chiba, Yoshiko Kasahara, Yukinari Kato, Mika Kato Kaneko, Atsushi Kuno, Hiromi Ito, Kazuo Kobayashi, Jun Hirabayashi, Yoshifumi Jigami and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

32 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Review
  3. Considerations for Glycoprotein Production.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Article
  5. Recombinant mucin biotechnology and engineering.Advanced drug delivery reviews · 2023
    Review
  6. Human Dectin-1 iseLife · 2022
    Article
  7. Review
  8. Engineering of Yeast Glycoprotein Expression.Advances in biochemical engineering/biotechnology · 2021
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. MammalianThe Journal of biological chemistry · 2017
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Using glyco-engineering to produce therapeutic proteins.Expert opinion on biological therapy · 2015
    Review
  19. Article
  20. Review
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

11 authors at 2 institutions in 1 country.

Koh AmanoResearch Center for Medical Glycoscience and Research Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology, 1-1-1 Higashi, Tsukuba 305-8566, Japan.
Yasunori Chiba
Yoshiko Kasahara
Yukinari Kato
Mika Kato Kaneko
Atsushi Kuno
Hiromi Ito
Kazuo Kobayashi
Jun Hirabayashi
Yoshifumi Jigami
Hisashi Narimatsu
National Institute of Advanced Industrial Science and Technology · JPKyowa Kirin (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mucin-type O-glycans are the most typical O-glycans found in mammalian cells and assume many different biological roles. Here, we report a genetic engineered yeast strain capable of producing mucin-type sugar chains. Genes encoding Bacillus subtilis UDP-Gal/GalNAc 4-epimerase, human UDP-Gal/GalNAc transporter, human ppGalNAc-T1, and Drosophila melanogaster core1 beta1-3 GalT were introduced into Saccharomyces cerevisiae. The engineered yeast was able to produce a MUC1a peptide containing O-glycan and also a mucin-like glycoprotein, human podoplanin (hPod; also known as aggrus), which is a platelet-aggregating factor that requires a sialyl-core1 structure for activity. After in vitro sialylation, hPod from yeast could induce platelet aggregation. Interestingly, substitution of ppGalNAc-T1 for ppGalNAc-T3 caused a loss of platelet aggregation-inducing activity, despite the fact that the sialyl-core1 was detectable in both hPod proteins on a lectin microarray. Most of O-mannosylation, a common modification in yeast, to MUC1a was suppressed by the addition of a rhodanine-3-acetic acid derivative in the culture medium. The yeast system we describe here is able to produce glycoproteins modified at different glycosylation sites and has the potential for use in basic research and pharmaceutical applications.

Indexed as

GlycoproteinsGlycosylationGlycosyltransferasesHumansMetabolic Networks and PathwaysMucinsProtein EngineeringYeastsGlycoproteinsGlycosyltransferasesMucins

Identifiers

PMID18296643
PMCPMC2265114
OpenAlexW2073581590

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.