ArticleNature communications2025
Control of Mycobacterium tuberculosis protein secretion by ESX-4 and the outer membrane EsxUT-EsxEF complex.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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.
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.
Who cites it
4 citing papers in PubMed.
- Construction of a subunit vaccine based on Mycobacterium tuberculosis EsxE and evaluation of its immunogenicity and ex vivo mycobacterial growth inhibitory activity.Archives of microbiology · 2026Article
- Article
- HowVaccines · 2026Review
- Loss of the ESX-5 secretion locus inProceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
- Update of
Authors and funding
6 authors.
Funding
Abstract
Mycobacterium tuberculosis uses five ESX systems to secrete effector proteins with distinct functions essential for the pathogen's growth and virulence. The current paradigm assumes that each ESX system secretes a distinct set of effector proteins. Here, we show that the EsxU-EsxT proteins, associated with the ESX-4 system, and the EsxE-EsxF proteins, encoded in the toxin operon cpnT, form a supercomplex that is required not only for toxin secretion, but also for outer membrane localization and for secretion of all Esx proteins into the cytosol of infected macrophages. Secretion of non-Esx proteins such as EspB, proteins involved in iron uptake, and PPE62, which are dependent on ESX-1, ESX-3 and ESX-5, respectively, also requires the EsxUT-EsxEF supercomplex. The mutual functional dependency of EsxEF and EsxUT on each other for outer-membrane localization synchronizes effector protein secretion, enabling M. tuberculosis to block phagosomal maturation and to permeabilize the phagosomal membrane when the pathogen is capable of killing host cells by toxin secretion. The requirement of the ESX-4 system for general secretion of ESX-dependent proteins in vivo is a critical vulnerability that could be targeted by drugs and/or in vaccines to simultaneously block many virulence factors of M. tuberculosis.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.