ArticlePLoS pathogens2014
The ESAT-6 protein of Mycobacterium tuberculosis interacts with beta-2-microglobulin (β2M) affecting antigen presentation function of macrophage.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
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Who cites it
96 citing papers in PubMed, 157 citations in OpenAlex.
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- Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Serum proteomic profiling of sepsis patients reveals a protein-based diagnostic model, with metabolomic insights into carbapenem-resistantFrontiers in immunology · 2026Article
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- Peripheral blood neutrophil proteomic profiling with transcriptomic data integration reveals biomarkers for tuberculosis infection diagnosis.EBioMedicine · 2025Article
- Immunoregulation by ESAT-6: From Pathogenesis of Tuberculosis to Potential Anti-Inflammatory and Anti-Rejection Application.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Diagnostic Accuracy of Novel Protein Biomarkers in Saliva to Detect Periodontitis Using Untargeted 'SWATH' Mass Spectrometry.Journal of clinical periodontology · 2025Article
- Global epidemiology of Mycobacterium tuberculosis lineage 4 insights from Ecuadorian genomic data.Scientific reports · 2025Article
- Evaluating single nucleotide polymorphisms in beta - 2 - microglobulin - a theoretical study.Frontiers in immunology · 2025Article
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- Characterisation of the periodontal proteome in gingival crevicular fluid and saliva using SWATH-MS.Frontiers in cellular and infection microbiology · 2025Article
- Evaluation of Immunostimulatory Effects of Bacterial Lysate Proteins on THP-1 Macrophages: Pro-inflammatory Cytokine Response and Proteomic Profiling.Journal of immunology research · 2025Article
- TowardMicroorganisms · 2024Review
- The SH3-binding domain of chorismate mutase protein ofiScience · 2024Article
- Optimizing antigen selection for the development of tuberculosis vaccines.Cell insight · 2024Review
- ESAT-6 undergoes self-association at phagosomal pH and an ESAT-6-specific nanobody restrictseLife · 2024Article
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36 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ESAT-6, an abundantly secreted protein of Mycobacterium tuberculosis (M. tuberculosis) is an important virulence factor, inactivation of which leads to reduced virulence of M. tuberculosis. ESAT-6 alone, or in complex with its chaperone CFP-10 (ESAT-6:CFP-10), is known to modulate host immune responses; however, the detailed mechanisms are not well understood. The structure of ESAT-6 or ESAT-6:CFP-10 complex does not suggest presence of enzymatic or DNA-binding activities. Therefore, we hypothesized that the crucial role played by ESAT-6 in the virulence of mycobacteria could be due to its interaction with some host cellular factors. Using a yeast two-hybrid screening, we identified that ESAT-6 interacts with the host protein beta-2-microglobulin (β2M), which was further confirmed by other assays, like GST pull down, co-immunoprecipitation and surface plasmon resonance. The C-terminal six amino acid residues (90-95) of ESAT-6 were found to be essential for this interaction. ESAT-6, in complex with CFP-10, also interacts with β2M. We found that ESAT-6/ESAT-6:CFP-10 can enter into the endoplasmic reticulum where it sequesters β2M to inhibit cell surface expression of MHC-I-β2M complexes, resulting in downregulation of class I-mediated antigen presentation. Interestingly, the ESAT-6:β2M complex could be detected in pleural biopsies of individuals suffering from pleural tuberculosis. Our data highlight a novel mechanism by which M. tuberculosis may undermine the host adaptive immune responses to establish a successful infection. Identification of such novel interactions may help us in designing small molecule inhibitors as well as effective vaccine design against tuberculosis.
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