Evidence map›Paper›PMID 27484084›Full record

ArticleBMC microbiology2016

ClpP-deletion impairs the virulence of Legionella pneumophila and the optimal translocation of effector proteins.

Bei-Bei Zhao, Xiang-Hui Li, Yong-Lun Zeng, Yong-Jun Lu

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 33 citations in OpenAlex.

  1. Journal of microbiology and biotechnology · 2025
    Article
  2. Article
  3. Development of heat-shock resistance inApplied and environmental microbiology · 2023
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. ClpP Protease, a Promising Antimicrobial Target.International journal of molecular sciences · 2019
    Review
  13. Article
  14. Article
  15. Reversible inhibition of the ClpP protease via an N-terminal conformational switch.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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

4 authors at 2 institutions in 1 country.

Bei-Bei ZhaoSchool of Life Sciences and Biomedical Center, Sun Yat-sen University, No. 135 Xingang road west, Guangzhou, 510275, China.
Xiang-Hui LiSchool of Life Sciences and Biomedical Center, Sun Yat-sen University, No. 135 Xingang road west, Guangzhou, 510275, China.
Yong-Lun ZengSchool of Life Sciences and Biomedical Center, Sun Yat-sen University, No. 135 Xingang road west, Guangzhou, 510275, China.
Yong-Jun LuSchool of Life Sciences and Biomedical Center, Sun Yat-sen University, No. 135 Xingang road west, Guangzhou, 510275, China. luyj@mail.sysu.edu.cn.
Sun Yat-sen University · CNChinese University of Hong Kong · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe opportunistic bacterial pathogen Legionella pneumophila uses substrate effectors of Dot/Icm type IVB secretion system (T4BSS) to accomplish survival and replication in amoebae cells and mammalian alveolar macrophages. During the conversion between its highly resistant, infectious dormant form and vigorously growing, uninfectious replicative form, L. pneumophila utilizes a complicated regulatory network in which proteolysis may play a significant role. As a highly conserved core protease, ClpP is involved in various cellular processes as well as virulence in bacteria, and has been proved to be required for the expression of transmission traits and cell division of L. pneumophila.

resultsThe clpP-deficient L. pneumophila strain failed to replicate and was digested in the first 3 h post-infection in mammalian cells J774A.1. Further investigation demonstrates that the clpP deficient mutant strain was unable to escape the endosome-lysosomal pathway in host cells. We also found that the clpP deficient mutant strain still expresses T4BSS components, induces contact-dependent cytotoxicity and translocate effector proteins RalF and LegK2, indicating that its T4BSS was overall functional. Interestingly, we further found that the translocation of several effector proteins is significantly reduced without ClpP.

conclusionsThe data indicate that ClpP plays an important role in regulating the virulence and effector translocation of Legionella pneumophila.

Indexed as

AnimalsBacterial ProteinsBacterial TranslocationCell LineEndocytosisEndopeptidase ClpEndosomesGuanine Nucleotide Exchange FactorsLegionella pneumophilaLysosomesMacrophagesMiceMutationPhagocytosisSequence DeletionVirulenceBacterial ProteinsEndopeptidase ClpGuanine Nucleotide Exchange FactorsRalF protein, Legionella pneumophilaClpPEffectorsLegionella pneumophilaSubstrateT4BSSTranslocationVirulence

Identifiers

PMID27484084
PMCPMC4969725
OpenAlexW2486659933

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.