ArticleNature communications2019
Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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Who cites it
18 citing papers in PubMed, 14 citations in OpenAlex.
- Live Cell Imaging of Chlamydia Inclusion Membrane Proteins Using Genetically Encoded Antibodies.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Inclusion Membrane Proteins ofMicroorganisms · 2026Review
- Chlamydia trachomatis orchestrates multifaceted host cell manipulation for immune evasion.Communications biology · 2026Review
- Minute-scale control of ubiquitin-mediated degradation reveals dynamics of bacterial secreted effector-functions.Nature communications · 2026Article
- CpoS-Inc interactions facilitate host cell modulation duringInfection and immunity · 2025Article
- Pathogenicity and virulence ofVirulence · 2025Review
- The Chlamydia effector Dre1 binds dynactin to reposition host organelles during infection.Cell reports · 2025Article
- Hijacking host cell vesicular transport: New insights into the nutrient acquisition mechanism ofVirulence · 2024Review
- Specialized contact sites regulate the fusion of chlamydial inclusion membranes.Nature communications · 2024Article
- Recognition ofInfection and immunity · 2024Article
- The Chlamydia trachomatis IncM Protein Interferes with Host Cell Cytokinesis, Centrosome Positioning, and Golgi Distribution and Contributes to the Stability of the Pathogen-Containing Vacuole.Infection and immunity · 2023Article
- Molecular pathogenesis ofFrontiers in cellular and infection microbiology · 2023Review
- Establishing the intracellular niche of obligate intracellular vacuolar pathogens.Frontiers in cellular and infection microbiology · 2023Review
- Microscopic Analysis of the Chlamydia abortus Inclusion and Its Interaction with Those Formed by Other Chlamydial Species.Infection and immunity · 2022Article
- Single-phagosome imaging reveals that homotypic fusion impairs phagosome degradative function.Biophysical journal · 2022Article
- Application of aJournal of bacteriology · 2021Article
- Got mutants? How advances in chlamydial genetics have furthered the study of effector proteins.Pathogens and disease · 2021Review
- The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019Review
Corrections and comments
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Authors and funding
10 authors at 1 institution in 2 countries.
Funding
Abstract
Many intracellular bacteria, including Chlamydia, establish a parasitic membrane-bound organelle inside the host cell that is essential for the bacteria's survival. Chlamydia trachomatis forms inclusions that are decorated with poorly characterized membrane proteins known as Incs. The prototypical Inc, called IncA, enhances Chlamydia pathogenicity by promoting the homotypic fusion of inclusions and shares structural and functional similarity to eukaryotic SNAREs. Here, we present the atomic structure of the cytoplasmic domain of IncA, which reveals a non-canonical four-helix bundle. Structure-based mutagenesis, molecular dynamics simulation, and functional cellular assays identify an intramolecular clamp that is essential for IncA-mediated homotypic membrane fusion during infection.
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Registered trials
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