Evidence map›Paper›PMID 35315684›Full record

ArticleJournal of bacteriology2022

Mycobacterium tuberculosis EspK Has Active but Distinct Roles in the Secretion of EsxA and EspB.

Ze Long Lim, Kylee Drever, Neeraj Dhar, Stewart T Cole, Jeffrey M Chen

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 12% 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, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Assembly of theMicrobiology spectrum · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Phase variation as a major mechanism of adaptation inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
  14. Proteo-genetic analysis reveals clear hierarchy of ESX-1 secretion inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. 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

5 authors at 3 institutions in 3 countries.

Ze Long LimVaccine and Infectious Disease Organization, Saskatoon, Canada.
Kylee DreverVaccine and Infectious Disease Organization, Saskatoon, Canada.
Neeraj DharVaccine and Infectious Disease Organization, Saskatoon, Canada.
Stewart T ColeInstitut Pasteurgrid.428999.7, Paris, France.ORCID 0000-0003-1400-5585
Jeffrey M ChenVaccine and Infectious Disease Organization, Saskatoon, Canada.ORCID 0000-0001-8431-3802
University of Saskatchewan · CAÉcole Polytechnique Fédérale de Lausanne · CHInstitut Pasteur · FR

Funding

European Community Seventh Framework Program 260872European Community Seventh Framework Program (FP7) 201762Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada (NSERC) 05730National Sanitarium Association (NSA)Swiss National Science Foundation 31003A-140778
6 · The paper itself

Abstract

The Mycobacterium tuberculosis type-7 protein secretion system ESX-1 is a major driver of its virulence. While the functions of most ESX-1 components are characterized, many others remain poorly defined. In this study, we examined the role of EspK, an ESX-1-associated protein that is thought to be dispensable for ESX-1 activity in members of the Mycobacterium tuberculosis complex. We show that EspK is needed for the timely and optimal secretion of EsxA and absolutely essential for EspB secretion in M. tuberculosis Erdman. We demonstrate that only the EsxA secretion defect can be alleviated in EspK-deficient M. tuberculosis by culturing it in media containing detergents like Tween 80 or tyloxapol. Subcellular fractionation experiments reveal EspK is exported by M. tuberculosis in an ESX-1-independent manner and localized to its cell wall. We also show a conserved W-X-G motif in EspK is important for its interaction with EspB and enabling its secretion. The same motif, however, is not important for EspK localization in the cell wall. Finally, we show EspB in EspK-deficient M. tuberculosis tends to adopt higher-order oligomeric conformations, more so than EspB in wild-type M. tuberculosis. These results suggest EspK interacts with EspB and prevents it from assembling prematurely into macromolecular complexes that are presumably too large to pass through the membrane-spanning ESX-1 translocon assembly. Collectively, our findings indicate M. tuberculosis EspK has a far more active role in ESX-1-mediated secretion than was previously appreciated and underscores the complex nature of this secretion apparatus.

Indexed as

Mycobacterium tuberculosisTuberculosisType VII Secretion SystemsBacterial ProteinsDetergentsHumansBacterial ProteinsDetergentsType VII Secretion SystemsEspKESX-1Mycobacterium tuberculosisprotein secretionvirulence

Identifiers

PMID35315684
PMCPMC9017330
OpenAlexW4220688447

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.