ArticleThe Journal of membrane biology2009
The influence of membrane lipids in Staphylococcus aureus gamma-hemolysins pore formation.
Article in The Journal of membrane biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 44 citations in OpenAlex.
- Identification and structural characterization of anthrax toxin receptor 2 as the Clostridium perfringens NetF receptor.Nature communications · 2026Article
- Staphylococcal toxin PVL ruptures model membranes under acidic conditions through interactions with cardiolipin and phosphatidic acid.PLoS biology · 2025Article
- Structural insights into lab-coevolved RNA-RBP pairs and applications of synthetic riboswitches in cell-free system.Nucleic acids research · 2025Article
- Gamma-Hemolysin Components: Computational Strategies for LukF-Hlg2 Dimer Reconstruction on a Model Membrane.International journal of molecular sciences · 2023Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Identification and Physicochemical Properties of the Novel Hemolysin(s) From Oral Secretions of Helicoverpa armigera (Lepidoptera: Noctuidae).Journal of insect science (Online) · 2021Article
- Structure-based discovery of a small-molecule inhibitor of methicillin-resistantThe Journal of biological chemistry · 2020Article
- Studying Staphylococcal Leukocidins: A Challenging Endeavor.Frontiers in microbiology · 2020Review
- Article
- Crystal structures of the components of the Staphylococcus aureus leukotoxin ED.Acta crystallographica. Section D, Structural biology · 2016Article
- Article
- The staphylococcal toxins γ-haemolysin AB and CB differentially target phagocytes by employing specific chemokine receptors.Nature communications · 2014Article
- The bicomponent pore-forming leucocidins of Staphylococcus aureus.Microbiology and molecular biology reviews : MMBR · 2014Review
- Article
- Molecular architecture and functional analysis of NetB, a pore-forming toxin from Clostridium perfringens.The Journal of biological chemistry · 2013Article
- Article
- Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- RNAi screen of Salmonella invasion shows role of COPI in membrane targeting of cholesterol and Cdc42.Molecular systems biology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The natural target of Staphylococcus aureus bicomponent gamma-hemolysins are leucocyte cell membranes. Because a proteinaceous receptor has not been found yet, we checked for the importance of the different membrane lipid compositions by measuring the activity of the toxin on several pure lipid model membranes. We investigated the effect of membrane thickness, fluidity, and presence of nonbilayer lipids and found that the toxin pore-forming ability increased in the presence of phosphocholines with short saturated acyl chains or with unsaturated chains even though not short. An increase of activity was also evident in the presence of cone-shaped lipids like phosphatidylethanolamine or diphytanoylphosphatidylcholine, whereas cylindrical lipids, like sphingomyelin, did not favor the activity. All these results suggest that gamma-hemolysins could bind to the bilayer only if the phosphatidylcholine (PC) head is freely accessible. This condition is satisfied by the concurrent presence of cholesterol and certain lipids, as highlighted by the so-called umbrella model (J. Huang and G. W. Feigenson, Biophys J 76:2142-2157, 1999). According to this model, cholesterol could help to a better exposition of PC head groups only if acyl chains are short or unsaturated. In fact, phosphatidylcholines with more than 13 carbon atoms acyl chains can cover cholesterol molecules; in this way, PC head groups pack tightly, rendering them inaccessible to the toxin, which thus shows a reduced pore-forming ability.
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.