Evidence map›Paper›PMID 37156500›Full record

ReviewJournal of molecular cell biology2023

Legionella pneumophila-mediated host posttranslational modifications.

Yi Yang, Ligang Mei, Jing Chen, Xiaorong Chen, Zhuolin Wang, Lu Liu, Aimin Yang

Open access · goldAbstract readReview
In one paragraph

Review in Journal of molecular cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

13 citing papers in PubMed, 12 citations in OpenAlex.

  1. Crystal structure of Legionella pneumophila glycosidase effector LegY.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  2. Article
  3. Article
  4. mBio · 2026
    Article
  5. Review
  6. Article
  7. Review
  8. Journal of bacteriology · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Insights into the role of legionella effectors on host metabolic perturbations.Frontiers in cellular and infection microbiology · 2024
    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

7 authors at 1 institution in 1 country.

Yi YangSchool of Life Sciences, Chongqing University, Chongqing 401331, China.
Ligang MeiSchool of Life Sciences, Chongqing University, Chongqing 401331, China.
Jing ChenSchool of Life Sciences, Chongqing University, Chongqing 401331, China.
Xiaorong ChenSchool of Life Sciences, Chongqing University, Chongqing 401331, China.
Zhuolin WangSchool of Life Sciences, Chongqing University, Chongqing 401331, China.
Lu LiuSchool of Life Sciences, Chongqing University, Chongqing 401331, China.
Aimin YangSchool of Life Sciences, Chongqing University, Chongqing 401331, China.ORCID 0000-0002-2240-5549
Chongqing University · CN

Funding

Fundamental Research Funds for the Central Universities 2022CDJYGRH-002National Natural Science Foundation of China 32170185Natural Science Foundation of Chongqing cstc2021jcyj-msxmX0030Venture and Innovation Support Program for Chongqing Overseas Returnees cx2022066
6 · The paper itself

Abstract

Legionella pneumophila is a Gram-negative bacterium ubiquitously present in freshwater environments and causes a serious type of pneumonia called Legionnaires' disease. During infections, L. pneumophila releases over 300 effector proteins into host cells through an Icm/Dot type IV secretion system to manipulate the host defense system for survival within the host. Notably, certain effector proteins mediate posttranslational modifications (PTMs), serving as useful approaches exploited by L. pneumophila to modify host proteins. Some effectors catalyze the addition of host protein PTMs, while others mediate the removal of PTMs from host proteins. In this review, we summarize L. pneumophila effector-mediated PTMs of host proteins, including phosphorylation, ubiquitination, glycosylation, AMPylation, phosphocholination, methylation, and ADP-ribosylation, as well as dephosphorylation, deubiquitination, deAMPylation, deADP-ribosylation, dephosphocholination, and delipidation. We describe their molecular mechanisms and biological functions in the regulation of bacterial growth and Legionella-containing vacuole biosynthesis and in the disruption of host immune and defense machinery.

Indexed as

Legionella pneumophilaLegionnaires' DiseaseHumansProtein Processing, Post-TranslationalUbiquitinationVacuolesbacterial effectorhost defense systemhost–pathogen interactionLegionella-containing vacuoleLegionella pneumophilapathogenesisposttranslational modification

Identifiers

PMID37156500
PMCPMC10720952
OpenAlexW4375955331

What Socratic holds

Textmetadata
LicenceCC BY-NC
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 Socratic graph.