Evidence map›Paper›PMID 30617292›Full record

ArticleNature chemical biology2019

Legionella effector SetA as a general O-glucosyltransferase for eukaryotic proteins.

Ling Gao, Qitao Song, Hao Liang, Yuntao Zhu, Tiantian Wei, Na Dong, Junyu Xiao, Feng Shao, Luhua Lai, Xing Chen

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Crystal structure of Legionella pneumophila glycosidase effector LegY.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  2. Review
  3. Structural insights into SetA-mediated Rab1 glucosylation and PI3P-guided localization during earlyProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Glycosylating Effectors ofBiomolecules · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Interfering with Autophagy: The Opposing Strategies Deployed byFrontiers in cellular and infection microbiology · 2020
    Review
  17. 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

10 authors at 2 institutions in 3 countries.

Ling GaoCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Qitao SongCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Hao LiangCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Yuntao ZhuCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Tiantian WeiPeking-Tsinghua Center for Life Sciences, Peking University, Beijing, China.
Na DongState Key Lab of Animal Nutrition, Ministry of Agriculture Feed Industry Center, China Agricultural University, Beijing, China.
Junyu XiaoPeking-Tsinghua Center for Life Sciences, Peking University, Beijing, China.ORCID http://orcid.org/0000-0003-1822-1701
Feng ShaoNational Institute of Biological Sciences, Beijing, China.ORCID http://orcid.org/0000-0002-9562-7791
Luhua LaiCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.ORCID http://orcid.org/0000-0002-8343-7587
Xing ChenCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China. xingchen@pku.edu.cn.ORCID http://orcid.org/0000-0002-3058-7370
Peking University · CNNational Institute of Biological Sciences, Beijing · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The identification of host protein substrates is key to understanding effector glycosyltransferases secreted by pathogenic bacteria and to using them for glycoprotein engineering. Here we report a chemical method for tagging, enrichment, and site-specific proteomic profiling of effector-modified proteins in host cells. Using this method, we discover that Legionella effector SetA α-O-glucosylates various eukaryotic proteins by recognizing a S/T-X-L-P/G sequence motif, which can be exploited to site-specifically introduce O-glucose on recombinant proteins.

Indexed as

Amino Acid SequenceBacterial ProteinsEukaryotaGlucosyltransferasesGlycosyltransferasesHost-Pathogen InteractionsLegionellaMonosaccharide Transport ProteinsProtein EngineeringProteomicsRecombinant ProteinsBacterial ProteinsGlucosyltransferasesGlycosyltransferasesMonosaccharide Transport ProteinsRecombinant Proteins

Identifiers

PMID30617292
OpenAlexW2904982639

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.