ArticleJournal of bacteriology2010
Coxiella burnetii expresses a functional Δ24 sterol reductase.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 41 citations in OpenAlex.
- Bacterial Puppeteering: How the Stealth BacteriumPathogens (Basel, Switzerland) · 2025Review
- Mechanisms of lipid homeostasis in the Coxiella Containing Vacuole.Biochemical Society transactions · 2025Review
- Untargeted Liquid Chromatography-High-Resolution Mass Spectrometry Metabolomic Investigation Reveals Altered Lipid Content inTropical medicine and infectious disease · 2024Article
- Cellular cholesterol licensesMicrobial cell (Graz, Austria) · 2023Article
- Genomic diversity and biosynthetic capabilities of sponge-associated chlamydiae.The ISME journal · 2022Article
- Lipid larceny: channelizing host lipids for establishing successful pathogenesis by bacteria.Virulence · 2021Review
- Coxiella burnetii and Related Tick Endosymbionts Evolved from Pathogenic Ancestors.Genome biology and evolution · 2021Article
- Modulation of Host Lipid Pathways by Pathogenic Intracellular Bacteria.Pathogens (Basel, Switzerland) · 2020Review
- Elevated Cholesterol in themBio · 2017Article
- Manipulation of Host Cholesterol by Obligate Intracellular Bacteria.Frontiers in cellular and infection microbiology · 2017Review
- Horizontally Acquired Biosynthesis Genes BoostFrontiers in cellular and infection microbiology · 2017Article
- Hijacking and Use of Host Lipids by Intracellular Pathogens.Microbiology spectrum · 2015Review
- Major differential gene regulation in Coxiella burnetii between in vivo and in vitro cultivation models.BMC genomics · 2015Article
- Article
- Virulent Coxiella burnetii pathotypes productively infect primary human alveolar macrophages.Cellular microbiology · 2013Article
- Lipid exchange between Borrelia burgdorferi and host cells.PLoS pathogens · 2013Article
- Bacterial colonization of host cells in the absence of cholesterol.PLoS pathogens · 2013Article
- Biosynthesis of cholesterol and other sterols.Chemical reviews · 2011Review
- Proteomics paves the way for Q fever diagnostics.Genome medicine · 2011Article
- Biogenesis of the lysosome-derived vacuole containing Coxiella burnetii.Microbes and infectionReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Coxiella burnetii, the etiological agent of human Q fever, occupies a unique niche inside the host cell, where it replicates in a modified acidic phagolysosome or parasitophorous vacuole (PV). The PV membrane is cholesterol-rich, and inhibition of host cholesterol metabolism negatively impacts PV biogenesis and pathogen replication. The precise source(s) of PV membrane cholesterol is unknown, as is whether the bacterium actively diverts and/or modifies host cell cholesterol or sterol precursors. C. burnetii lacks enzymes for de novo cholesterol biosynthesis; however, the organism encodes a eukaryote-like Δ24 sterol reductase homolog, CBU1206. Absent in other prokaryotes, this enzyme is predicted to reduce sterol double bonds at carbon 24 in the final step of cholesterol or ergosterol biosynthesis. In the present study, we examined the functional activity of CBU1206. Amino acid alignments revealed the greatest sequence identity (51.7%) with a Δ24 sterol reductase from the soil amoeba Naegleria gruberi. CBU1206 activity was examined by expressing the protein in a Saccharomyces cerevisiae erg4 mutant under the control of a galactose-inducible promoter. Erg4 is a yeast Δ24 sterol reductase responsible for the final reduction step in ergosterol synthesis. Like Erg4-green fluorescent protein (GFP), a CBU1206-GFP fusion protein localized to the yeast endoplasmic reticulum. Heterologous expression of CBU1206 rescued S. cerevisiae erg4 sensitivity to growth in the presence of brefeldin A and cycloheximide and resulted in new synthesis of ergosterol. These data indicate CBU1206 is an active sterol reductase and suggest the enzyme may act on host sterols during C. burnetii intracellular growth.
Indexed as
Identifiers
What OpenQuestion holds
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.