ArticlePathogens and disease2017
The Coxiella Burnetii type IVB secretion system (T4BSS) component DotA is released/secreted during infection of host cells and during in vitro growth in a T4BSS-dependent manner.
Article in Pathogens and disease, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Type IV Secretion System Drives Lipid Mixing.bioRxiv : the preprint server for biology · 2026Article
- A Comprehensive Review of the Mechanisms of Human Q Fever: Pathogenesis and Pathophysiology.Pathogens (Basel, Switzerland) · 2025Review
- The Passage of Chaperonins to Extracellular Locations inBiomolecules · 2025Article
- CRISPR-Cas9-based approaches for genetic analysis and epistatic interaction studies inmSphere · 2024Article
- Morphological remodeling ofiScience · 2023Article
- Comparative Transcriptomics and Genomics from Continuous Axenic Media Growth IdentifiesbioRxiv : the preprint server for biology · 2023Article
- Proteome-wide analysis of Coxiella burnetii for conserved T-cell epitopes with presentation across multiple host species.BMC bioinformatics · 2021Article
- Sequence of a Coxiella Endosymbiont of the Tick Amblyomma nuttalli Suggests a Pattern of Convergent Genome Reduction in the Coxiella Genus.Genome biology and evolution · 2021Article
- Article
- Quantitative Proteome Profiling ofFrontiers in microbiology · 2019Article
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Authors and funding
4 authors.
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Abstract
Coxiella burnetii is a Gram-negative intracellular pathogen and is the causative agent of the zoonotic disease Q fever. To cause disease, C. burnetii requires a functional type IVB secretion system (T4BSS) to transfer effector proteins required for the establishment and maintenance of a membrane-bound parasitophorous vacuole (PV) and further modulation of host cell process. However, it is not clear how the T4BSS interacts with the PV membrane since neither a secretion pilus nor an extracellular pore forming apparatus has not been described. To address this, we used the acidified citrate cysteine medium (ACCM) along with cell culture infection and immunological techniques to identify the cellular and extracellular localization of T4BSS components. Interestingly, we found that DotA and IcmX were secreted/released in a T4BSS-dependent manner into the ACCM. Analysis of C. burnetii-infected cell lines revealed that DotA colocalized with the host cell marker CD63 (LAMP3) at the PV membrane. In the absence of bacterial protein synthesis, DotA also became depleted from the PV membrane. These data are the first to identify the release/secretion of C. burnetii T4BSS components during axenic growth and the interaction of a T4BSS component with the PV membrane during infection of host cells.
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