ArticleThe Journal of biological chemistry2014
An α-helical core encodes the dual functions of the chlamydial protein IncA.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Ectopic overexpression and CRISPRi-based knockdown ofJournal of bacteriology · 2025Article
- CpoS-Inc interactions facilitate host cell modulation duringInfection and immunity · 2025Article
- Pathogenicity and virulence ofVirulence · 2025Review
- 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
- Intracellular lifestyle of Chlamydia trachomatis and host-pathogen interactions.Nature reviews. Microbiology · 2023Review
- Establishing the intracellular niche of obligate intracellular vacuolar pathogens.Frontiers in cellular and infection microbiology · 2023Review
- Got mutants? How advances in chlamydial genetics have furthered the study of effector proteins.Pathogens and disease · 2021Review
- 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
- Article
- Manipulation of Host Cell Organelles by Intracellular Pathogens.Microbiology spectrum · 2019Review
- Both the N- and C- terminal regions of the Chlamydial inclusion protein D (IncD) are required for interaction with the pleckstrin homology domain of the ceramide transport protein CERT.Biochemical and biophysical research communications · 2018Article
- Subversion of the Endocytic and Secretory Pathways by Bacterial Effector Proteins.Frontiers in cell and developmental biology · 2018Review
- Article
- A Co-infection Model System and the Use of Chimeric Proteins to StudyFrontiers in cellular and infection microbiology · 2017Article
- Chlamydia cell biology and pathogenesis.Nature reviews. Microbiology · 2016Review
- A Functional Core of IncA Is Required for Chlamydia trachomatis Inclusion Fusion.Journal of bacteriology · 2016Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Chlamydia is an intracellular bacterium that establishes residence within parasitophorous compartments (inclusions) inside host cells. Chlamydial inclusions are uncoupled from the endolysosomal pathway and undergo fusion with cellular organelles and with each other. To do so, Chlamydia expresses proteins on the surface of the inclusion using a Type III secretion system. These proteins, termed Incs, are located at the interface between host and pathogen and carry out the functions necessary for Chlamydia survival. Among these Incs, IncA plays a critical role in both protecting the inclusion from lysosomal fusion and inducing the homotypic fusion of inclusions. Within IncA are two regions homologous to eukaryotic SNARE (soluble N-ethylmaleimide-sensitive factor attachment receptor) domains referred to as SNARE-like domain 1 (SLD1) and SNARE-like domain 2 (SLD2). Using a multidisciplinary approach, we have discovered the functional core of IncA that retains the ability to both inhibit SNARE-mediated fusion and promote the homotypic fusion of Chlamydia inclusions. Circular dichroism and analytical ultracentrifugation experiments show that this core region is composed almost entirely of α-helices and assembles into stable homodimers in solution. Altogether, we propose that both IncA functions are encoded in a structured core domain that encompasses SLD1 and part of SLD2.
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