ArticleBiophysical journal2016
Ordered Membrane Domain-Forming Properties of the Lipids of Borrelia burgdorferi.
Article in Biophysical journal, 2016. 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
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
11 citing papers in PubMed, 17 citations in OpenAlex.
- Lipid scavenging by the Lyme disease spirochete Borrelia burgdorferi.PLoS pathogens · 2025Article
- Sterol-lipids enable large-scale, liquid-liquid phase separation in bilayer membranes of only two components.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Adjustment in the Composition and Organization ofInternational journal of molecular sciences · 2023Article
- Membrane Organization Strategies in Vesicular Antibiotic Delivery.The Journal of membrane biology · 2022Review
- Lyme Disease in Humans.Current issues in molecular biology · 2021Article
- Structure, metabolism and biological functions of steryl glycosides in mammals.The Biochemical journal · 2020Review
- Structural and Functional Analysis of BBA03,Pathogens (Basel, Switzerland) · 2020Article
- Helicobacter pylori lipids can form ordered membrane domains (rafts).Biochimica et biophysica acta. Biomembranes · 2019Article
- Lamellar Phases Composed of Phospholipid, Cholesterol, and Ceramide, as Studied byBiophysical journal · 2019Article
- Reorganization of Ternary Lipid Mixtures of Nonphosphorylated Phosphatidylinositol Interacting with Angiomotin.The journal of physical chemistry. B · 2018Article
- Lipid rafts can form in the inner and outer membranes of Borrelia burgdorferi and have different properties and associated proteins.Molecular microbiology · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Co-existing disordered and ordered (raft) membrane domains exist in Borrelia burgdorferi, the causative agent of Lyme disease. However, although B. burgdorferi contains cholesterol lipids, it lacks sphingolipids-a crucial component of rafts in eukaryotes. To define the principles of ordered lipid domain formation in Borrelia, the domain forming properties of vesicles composed of its three major lipids, acylated cholesteryl galactoside (ACGal), monogalactosyl diacyglycerol (MGalD), and phosphatidylcholine (PC) and/or their mixtures were studied. Anisotropy and fluorescence resonance energy transfer measurements were used to assay membrane order and ordered-domain formation. ACGal had the highest potential to form ordered domains. Interestingly, mixtures of ACGal with B. burgdorferi PC formed ordered domains more readily than mixtures of ACGal with MGalD. This appears to reflect the relatively high level of saturation observed for B. burgdorferi PC, as vesicles containing ACGal and PC, but in which the unsaturated lipid dioleoyl PC was substituted for Borrelia PC, failed to form ordered domains. In addition, the properties of ACGal were compared to those of cholesterol. Depending on what other lipids were present, ordered-domain formation in the presence of ACGal was greater than or equal to that in the presence of cholesterol. Giant unilamellar vesicles formed from ACGal-containing mixtures showed rounded domain shapes similar to those in analogous vesicles containing cholesterol, indicative of liquid-ordered state rather than solid-like gel-state domain formation. Over all, principles of ordered-domain formation in B. burgdorferi appear to be very similar to those in eukaryotes, with saturated PC taking the place of sphingolipids, but with ACGal being the main lipid component inducing ordered-domain formation.
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.