ArticleMicrobiology spectrum2023
Chlamydia trachomatis Subverts Alpha-Actinins To Stabilize Its Inclusion.
Article in Microbiology spectrum, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 10 citations in OpenAlex.
- Split-GFP Reporter-Based Detection of Chlamydia trachomatis Inclusion Damage.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Inclusion Membrane Proteins ofMicroorganisms · 2026Review
- An Exploratory In Silico Analysis ofCancers · 2026Article
- Minute-scale control of ubiquitin-mediated degradation reveals dynamics of bacterial secreted effector-functions.Nature communications · 2026Article
- Exploring microorganism-host interactions: Emerging organoid models and analytical approaches.mLife · 2026Review
- Pathogenicity and virulence ofVirulence · 2025Review
- Genome-wide identification of modulators of Chlamydia trachomatis parasitophorous vacuole stability highlights an important role for sphingolipid supply.PLoS biology · 2025Article
- TheJournal of bacteriology · 2025Article
- Genome-wide association study of chlamydia reinfection in African American women.Frontiers in immunology · 2025Article
- Specialized contact sites regulate the fusion of chlamydial inclusion membranes.Nature communications · 2024Article
- The emerging complexity of Chlamydia trachomatis interactions with host cells as revealed by molecular genetic approaches.Current opinion in microbiology · 2023Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Chlamydia trachomatis is the leading cause of sexually transmitted bacterial disease and a global health burden. As an obligate intracellular pathogen, Chlamydia has evolved many strategies to manipulate its host and establish its intracellular niche called the inclusion. C. trachomatis reorganizes the host actin cytoskeleton to form scaffolds around the inclusion and reinforce the growing inclusion membrane. To control the kinetics and formation of actin scaffolds, Chlamydia expresses the effector InaC/CT813, which activates the host GTPase RhoA. Here, we have discovered that InaC stabilizes actin scaffolds through the host actin cross-linking proteins α-actinins 1 and 4. We demonstrate that α-actinins are recruited to the inclusion membrane in an InaC-dependent manner and associate with actin scaffolds that envelop the inclusion. Small interfering RNA (siRNA)-mediated knockdown of α-actinins differentially regulate the frequency of actin scaffolds and impair inclusion stability, leaving them susceptible to rupture and to nonionic detergent extraction. Overall, our data identify new host effectors that are subverted by InaC to stabilize actin scaffolds, highlighting the versatility of InaC as a key regulator of the host cytoskeletal network during Chlamydia 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.