ArticlePloS one2013
Two coiled-coil domains of Chlamydia trachomatis IncA affect membrane fusion events during infection.
Article in PloS one, 2013. 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, 48 citations in OpenAlex.
- Transmembrane effector substrates of type IV secretion systems: mechanisms of secretion and insertion into host cell membranes.microLife · 2026Review
- CpoS-Inc interactions facilitate host cell modulation duringInfection and immunity · 2025Article
- Pathogenicity and virulence ofVirulence · 2025Review
- Emerging Insights into Protein Post-Translational Modifications in Chlamydia-Host Interactions.The American journal of pathology · 2025Review
- Inc/GFP chimera protein-based interactomics reveals host cellular interactions of Cps0558, a novel Chlamydia psittaci inclusion protein.Pathogens and disease · 2025Article
- Specialized contact sites regulate the fusion of chlamydial inclusion membranes.Nature communications · 2024Article
- Recognition ofInfection and immunity · 2024Article
- Transmembrane substrates of type three secretion system injectisomes.Microbiology (Reading, England) · 2023Review
- Got mutants? How advances in chlamydial genetics have furthered the study of effector proteins.Pathogens and disease · 2021Review
- Eukaryotic SNARE VAMP3 Dynamically Interacts with Multiple Chlamydial Inclusion Membrane Proteins.Infection and immunity · 2021Article
- The Hypothetical Inclusion Membrane Protein CPSIT_0846 Regulates Mitochondrial-Mediated Host Cell ApoptosisFrontiers in cellular and infection microbiology · 2021Article
- Proximity Labeling To Map Host-Pathogen Interactions at the Membrane of a Bacterium-Containing Vacuole in Chlamydia trachomatis-Infected Human Cells.Infection and immunity · 2019Article
- The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019Review
- Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA.Nature communications · 2019Article
- A primary study on genes with selected mutations by in vitro passage of Chlamydia muridarum strains.Pathogens and disease · 2019Article
- Manipulation of Host Cell Organelles by Intracellular Pathogens.Microbiology spectrum · 2019Review
- Chlamydial Infection From Outside to Inside.Frontiers in microbiology · 2019Review
- Subversion of the Endocytic and Secretory Pathways by Bacterial Effector Proteins.Frontiers in cell and developmental biology · 2018Review
- A Co-infection Model System and the Use of Chimeric Proteins to StudyFrontiers in cellular and infection microbiology · 2017Article
- Development of a Proximity Labeling System to Map theFrontiers in cellular and infection microbiology · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Chlamydia trachomatis replicates in a parasitophorous membrane-bound compartment called an inclusion. The inclusions corrupt host vesicle trafficking networks to avoid the degradative endolysosomal pathway but promote fusion with each other in order to sustain higher bacterial loads in a process known as homotypic fusion. The Chlamydia protein IncA (Inclusion protein A) appears to play central roles in both these processes as it participates to homotypic fusion and inhibits endocytic SNARE-mediated membrane fusion. How IncA selectively inhibits or activates membrane fusion remains poorly understood. In this study, we analyzed the spatial and molecular determinants of IncA's fusogenic and inhibitory functions. Using a cell-free membrane fusion assay, we found that inhibition of SNARE-mediated fusion requires IncA to be on the same membrane as the endocytic SNARE proteins. IncA displays two coiled-coil domains showing high homology with SNARE proteins. Domain swap and deletion experiments revealed that although both these domains are capable of independently inhibiting SNARE-mediated fusion, these two coiled-coil domains cooperate in mediating IncA multimerization and homotypic membrane interaction. Our results support the hypothesis that Chlamydia employs SNARE-like virulence factors that positively and negatively affect membrane fusion and promote infection.
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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.