ArticleMolecular microbiology2012
Polar assembly and scaffolding proteins of the virulence-associated ESX-1 secretory apparatus in mycobacteria.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 35 citations in OpenAlex.
- Type VII secretion system gene mutations driving global mycobacterium tuberculosis transmission revealed by whole genomic sequence.Frontiers in cellular and infection microbiology · 2025Article
- ESAT-6 a Major Virulence Factor ofBiomolecules · 2023Review
- Host-directed therapy against tuberculosis: Concept and recent developments.Journal of biosciences · 2023Review
- Localization of EccABMC microbiology · 2022Article
- Intracellular localization of the mycobacterial stressosome complex.Scientific reports · 2021Article
- Article
- The final assembly of trehalose polyphleates takes place within the outer layer of the mycobacterial cell envelope.The Journal of biological chemistry · 2020Article
- Polarly Localized EccEJournal of bacteriology · 2020Article
- WhiB6 regulation of ESX-1 gene expression is controlled by a negative feedback loop inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Esx Systems and the Mycobacterial Cell Envelope: What's the Connection?Journal of bacteriology · 2017Review
- Polar delivery ofProceedings of the National Academy of Sciences of the United States of America · 2017Article
- The plasmid-mediated evolution of the mycobacterial ESX (Type VII) secretion systems.BMC evolutionary biology · 2016Article
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- Article
- How do bacteria localize proteins to the cell pole?Journal of cell science · 2014Review
- Distributive conjugal transfer in mycobacteria generates progeny with meiotic-like genome-wide mosaicism, allowing mapping of a mating identity locus.PLoS biology · 2013Article
- Article
- Virulence factors of the Mycobacterium tuberculosis complex.Virulence · 2013Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
The ESX-1 secretion system is required for pathogenicity of Mycobacterium tuberculosis (Mtb). Despite considerable research, little is known about the structural components of ESX-1, or how these proteins are assembled into the active secretion apparatus. Here, we exploit the functionally related ESX-1 apparatus of Mycobacterium smegmatis (Ms) to show that fluorescently tagged proteins required for ESX-1 activity consistently localize to the cell pole, identified by time-lapse fluoro-microscopy as the non-septal (old) pole. Deletions in Msesx1 prevented polar localization of tagged proteins, indicating the need for specific protein-protein interactions in polar trafficking. Remarkably, expression of the Mtbesx1 locus in Msesx1 mutants restored polar localization of tagged proteins, indicating establishment of the MtbESX-1 apparatus in M. smegmatis. This observation illustrates the cross-species conservation of protein interactions governing assembly of ESX-1, as well as polar localization. Importantly, we describe novel non-esx1-encoded proteins, which affect ESX-1 activity, which colocalize with ESX-1, and which are required for ESX-1 recruitment and assembly. This analysis provides new insights into the molecular assembly of this important determinant of Mtb virulence.
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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.