ArticleCell reports2025
Real-time visualization reveals Mycobacterium tuberculosis ESAT-6 disrupts phagosome-like compartment via fibril-mediated vesiculation.
Article in Cell reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- EspF acts as a molecular scaffold to facilitate TRIM25-mediated NLRP3 inflammasome activation during mycobacterial infection.Virulence · 2026Article
- Mycobacterial surface-mediated mechanical priming initiates spacious to compact phagosome switching for egress.iScience · 2026Article
- Targeting cGAS-STING signaling to overcome antibiotic-resistant bacterial infections: Challenges and opportunities.Science advances · 2026Review
- Membrane interfacial potential governs surface condensation and fibrillation of α-Synuclein in neurons.Nature communications · 2026Article
- Membrane microdomains are crucial forScience advances · 2026Article
- Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Recent Characterization of Key Proteins to Combat Tuberculosis.Advances in experimental medicine and biology · 2026Review
- ESAT-6 and CFP-10 reactive IgG in patients with tuberculosis inhibits intracellular bacteria.Cell reports · 2025Article
- An ER-resident lipid scramblase is crucial for biogenesis and function of apicomplexan parasite secretory organelles.Nature communications · 2025Article
- Advances in Host-Pathogen Interactions in Tuberculosis: Emerging Strategies for Therapeutic Intervention.International journal of molecular sciences · 2025Review
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Authors and funding
10 authors.
Funding
Abstract
Mycobacterium tuberculosis (Mtb) evades host defense by hijacking and rupturing the phagosome. ESAT-6, a secreted virulence protein of Mtb, is known to be critical for phagosome rupture. However, the mechanism of ESAT-6-mediated disruption of the phagosomal membrane remains unknown. Using in vitro reconstitution, live-cell imaging, and numerical simulations, we discover that ESAT-6 polymerization forces remodeling and vesiculation of the phagosome-like compartment both in vitro and in vivo. Shallow insertion of ESAT-6 leads to tubular and bud-like deformations on the membrane facilitated by a reduction in membrane tension. Growing fibrils generate both radial and tangential forces causing local remodeling and shape transition of the membrane into buds. The ESAT-6-bound tensed membrane undergoes local changes in membrane curvature and lipid phase separation that assist the subsequent fission. Overall, the findings provide mechanistic insights into the long-standing question of phagosome disruption by Mtb for its escape.
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Registered trials
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