ArticleJournal of structural biology2015
Structure of EspB, a secreted substrate of the ESX-1 secretion system of Mycobacterium tuberculosis.
Article in Journal of structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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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.
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Who cites it
28 citing papers in PubMed, 56 citations in OpenAlex.
- Future Research Directions on Mycobacterium tuberculosis Proteins.Advances in experimental medicine and biology · 2026Review
- Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- A widespread family of molecular chaperones promotes the intracellular stability of type VIIb secretion system-exported toxins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Generation of novel polyclonal antibodies against Mycobacterium tuberculosis lipoarabinomannan, EspB, and Mtb8.Applied microbiology and biotechnology · 2025Article
- PPE50 variants as novel phylogeographic signatures of host-pathogen co-evolution in tuberculosis.Communications biology · 2025Article
- Interbacterial competition mediated by the type VIIb secretion system.Microbiology (Reading, England) · 2023Review
- Article
- Uptake-independent killing of macrophages by extracellular Mycobacterium tuberculosis aggregates.The EMBO journal · 2023Article
- Cryo-EM reveals the membrane-binding phenomenon of EspB, a virulence factor of the mycobacterial type VII secretion system.The Journal of biological chemistry · 2023Article
- The ESX-1 Substrate PPE68 Has a Key Function in ESX-1-Mediated Secretion in Mycobacterium marinum.mBio · 2022Article
- Mycobacterium tuberculosis EspK Has Active but Distinct Roles in the Secretion of EsxA and EspB.Journal of bacteriology · 2022Article
- The Type VII Secretion System ofAnnual review of microbiology · 2021Article
- Type VII secretion systems: structure, functions and transport models.Nature reviews. Microbiology · 2021Review
- Microarray-based selection of a serum biomarker panel that can discriminate between latent and active pulmonary TB.Scientific reports · 2021Article
- Recent Insights into the Structure and Function of Mycobacterial Membrane Proteins Facilitated by Cryo-EM.The Journal of membrane biology · 2021Review
- Priming mycobacterial ESX-secreted protein B to form a channel-like structure.Current research in structural biology · 2021Article
- PE5-PPE4-EspGThe Journal of biological chemistry · 2020Article
- Modification of a PE/PPE substrate pair reroutes an Esx substrate pair from the mycobacterial ESX-1 type VII secretion system to the ESX-5 system.The Journal of biological chemistry · 2020Article
- High resolution CryoEM structure of the ring-shaped virulence factor EspB fromJournal of structural biology: X · 2020Article
- Cloning, Expression and Purification of Espc, Espb and Espc/Espb Proteins ofReports of biochemistry & molecular biology · 2020Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Mycobacterium tuberculosis secretes multiple virulence factors during infection via the general Sec and Tat pathways, and via specialized ESX secretion systems, also referred to as type VII secretion systems. The ESX-1 secretion system is an important virulence determinant because deletion of ESX-1 leads to attenuation of M. tuberculosis. ESX-1 secreted protein B (EspB) contains putative PE (Pro-Glu) and PPE (Pro-Pro-Glu) domains, and a C-terminal domain, which is processed by MycP1 protease during secretion. We determined the crystal structure of PE-PPE domains of EspB, which represents an all-helical, elongated molecule closely resembling the structure of the PE25-PPE41 heterodimer despite limited sequence similarity. Also, we determined the structure of full-length EspB, which does not have interpretable electron density for the C-terminal domain confirming that it is largely disordered. Comparative analysis of EspB in cell lysate and culture filtrates of M. tuberculosis revealed that mature secreted EspB forms oligomers. Electron microscopy analysis showed that the N-terminal fragment of EspB forms donut-shaped particles. These data provide a rationale for the future investigation of EspB's role in M. tuberculosis pathogenesis.
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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.