Evidence map›Paper›PMID 40659784›Full record

ArticleNature chemical biology2025

Protein β-O-glucosylation by Legionella LtpM through short consensus sequons G-T/S and S-G.

Wei Li, Ling Gao, Shiyong Cui, Tiantian Wei, Jiayu Sun, Xinyue Zhou, Shuyu Liang, Xiaoqing Pan, Xuanzhen Pan, Chuanping Gao and 7 more

Abstract read
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In one paragraph

Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Crystal structure of Legionella pneumophila glycosidase effector LegY.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  2. Review
  3. 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

17 authors.

Wei Li *College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Ling Gao *College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Shiyong Cui *College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Tiantian Wei *Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, China.
Jiayu SunCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Xinyue ZhouCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Shuyu LiangCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Xiaoqing PanCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Xuanzhen PanSchool of Pharmaceutical Sciences, Tsinghua University, Beijing, China.
Chuanping GaoSchool of Life Sciences, Peking University, Beijing, China.ORCID http://orcid.org/0000-0002-7654-9476
Yingze WangCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Junhan ChangCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Chunting WangCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Pinou LvCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Junyu XiaoPeking-Tsinghua Center for Life Sciences, Peking University, Beijing, China. junyuxiao@pku.edu.cn.ORCID http://orcid.org/0000-0003-1822-1701
Peng DaiCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China. pengdai@pku.edu.cn.ORCID http://orcid.org/0000-0002-4581-3473
Xing ChenCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China. xingchen@pku.edu.cn.ORCID http://orcid.org/0000-0002-3058-7370

Funding

National Natural Science Foundation of China (National Science Foundation of China) 22037001National Natural Science Foundation of China (National Science Foundation of China) 22377002National Natural Science Foundation of China (National Science Foundation of China) 32325018
6 · The paper itself

Abstract

Unlike N-glycosylation, protein O-glycosylation often lacks a strict consensus sequon, making synthesis of homogeneous O-glycoproteins and site-specific engineering of O-glucosylation challenging. Here we identify Legionella effector LtpM as a versatile protein β-O-glucosyltransferase recognizing extremely short two-residue sequons G-T/S and S-G. X-ray crystallography, molecular simulation and biochemical studies together reveal a unique catalytic mechanism: four residues of LtpM (F166, Q167, W228 and K225) serve as 'gatekeepers' above the binding pocket of the uridine diphosphate (UDP)-glucose sugar donor to form a narrow clamp for the substrate proteins, limiting the residue adjacent to serine or threonine to be exclusively glycine. By exploiting the short sequons, LtpM is developed as a powerful tool for site-specifically O-glucosylating various eukaryotic proteins of interest. In particular, O-glucose serves as a functional surrogate for O-linked N-acetylglucosamine in a synaptic Ras GTPase-activating protein. Additionally, LtpM accepts 6-azido analog of UDP-glucose and enables site-specific bioorthogonal conjugation of proteins.

Indexed as

Bacterial ProteinsGlucosyltransferasesLegionellaCrystallography, X-RayGlycosylationModels, MolecularBacterial ProteinsGlucosyltransferases

Identifiers

PMID40659784

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Registered trials

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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.