ArticlePLoS pathogens2007
A mycobacterium ESX-1-secreted virulence factor with unique requirements for export.
Article in PLoS pathogens, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.
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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.
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Who cites it
122 citing papers in PubMed, 199 citations in OpenAlex.
- Epigenetic Reprogramming byAntibiotics (Basel, Switzerland) · 2026Review
- Article
- Tyloxapol inhibits ESX-1 secretion inJournal of bacteriology · 2026Article
- Protein Architecture and Composition in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Generation of novel polyclonal antibodies against Mycobacterium tuberculosis lipoarabinomannan, EspB, and Mtb8.Applied microbiology and biotechnology · 2025Article
- Review
- TnSeq identifies genetic requirements of Mycobacterium tuberculosis for survival under vaccine-induced immunity.NPJ vaccines · 2025Article
- In vivo regulation of the monocyte phenotype by Mycobacterium marinum and the ESX-1 type VII secretion system.Scientific reports · 2025Article
- Exploring host-pathogen interactions in the Dictyostelium discoideum-Mycobacterium marinum infection model of tuberculosis.Disease models & mechanisms · 2024Review
- New insight in molecular detection of Mycobacterium tuberculosis.AMB Express · 2024Review
- The loss of the PDIM/PGL virulence lipids causes differential secretion of ESX-1 substrates inmSphere · 2024Article
- The antagonistic transcription factors, EspM and EspN, regulate the ESX-1 secretion system inmBio · 2024Article
- A novel variant of theMicrobial genomics · 2023Article
- An N-acetyltransferase required for EsxA N-terminal protein acetylation and virulence in Mycobacterium marinum.bioRxiv : the preprint server for biology · 2023Article
- EspB and HtpG interact with the type III-A CRISPR/Cas system ofFrontiers in molecular biosciences · 2023Article
- Evaluation of the Immunogenicity of Recombinant Espb, Espc Proteins fromReports of biochemistry & molecular biology · 2023Article
- The ESX-1 Substrate PPE68 Has a Key Function in ESX-1-Mediated Secretion in Mycobacterium marinum.mBio · 2022Article
- Proteo-genetic analysis reveals clear hierarchy of ESX-1 secretion inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Mycobacterium tuberculosis EspK Has Active but Distinct Roles in the Secretion of EsxA and EspB.Journal of bacteriology · 2022Article
- Article
62 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Specialized secretion systems of pathogenic bacteria commonly transport multiple effectors that act in concert to control and exploit the host cell as a replication-permissive niche. Both the Mycobacterium marinum and the Mycobacterium tuberculosis genomes contain an extended region of difference 1 (extRD1) locus that encodes one such pathway, the early secretory antigenic target 6 (ESAT-6) system 1 (ESX-1) secretion apparatus. ESX-1 is required for virulence and for secretion of the proteins ESAT-6, culture filtrate protein 10 (CFP-10), and EspA. Here, we show that both Rv3881c and its M. marinum homolog, Mh3881c, are secreted proteins, and disruption of RD1 in either organism blocks secretion. We have renamed the Rv3881c/Mh3881c gene espB for ESX-1 substrate protein B. Secretion of M. marinum EspB (EspBM) requires both the Mh3879c and Mh3871 genes within RD1, while CFP-10 secretion is not affected by disruption of Mh3879c. In contrast, disruption of Mh3866 or Mh3867 within the extRD1 locus prevents CFP-10 secretion without effect on EspBM. Mutants that fail to secrete only EspBM or only CFP-10 are less attenuated in macrophages than mutants failing to secrete both substrates. EspBM physically interacts with Mh3879c; the M. tuberculosis homolog, EspBT, physically interacts with Rv3879c; and mutants of EspBM that fail to bind Mh3879c fail to be secreted. We also found interaction between Rv3879c and Rv3871, a component of the ESX-1 machine, suggesting a mechanism for the secretion of EspB. The results establish EspB as a substrate of ESX-1 that is required for virulence and growth in macrophages and suggests that the contribution of ESX-1 to virulence may arise from the secretion of multiple independent substrates.
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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.