ArticleJournal of molecular biology2014
Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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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.
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Who cites it
39 citing papers in PubMed, 70 citations in OpenAlex.
- Epitope Mapping with Sidewinder: An XL-MS and Structural Modeling Approach.International journal of molecular sciences · 2025Article
- Advances in Necrotizing Fasciitis Animal Models: Current Trends and Future Perspectives.Journal of inflammation research · 2025Review
- Streptolysin O accelerates the conversion of plasminogen to plasmin.Nature communications · 2024Article
- Multimodal Mass Spectrometry Identifies a Conserved Protective Epitope inAnalytical chemistry · 2024Article
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- Some Examples of Bacterial Toxins as Tools.Toxins · 2024Review
- Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024Review
- Development and characterization of a hemolysis inhibition assay to determine functionality of anti-Streptolysin O antibodies in human sera.Journal of immunological methods · 2024Article
- Hypo-Osmotic Stress and Pore-Forming Toxins Adjust the Lipid Order in Sheep Red Blood Cell Membranes.Membranes · 2023Article
- A smart pathogen detector engineered from intracellular hydrogelation of DNA-decorated macrophages.Nature communications · 2023Article
- Visualizing the Domino-Like Prepore-to-Pore Transition of Streptolysin O by High-Speed AFM.The Journal of membrane biology · 2023Article
- Structural basis underlying the synergism of NADase and SLO during group A Streptococcus infection.Communications biology · 2023Article
- Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Luteolin Binds Streptolysin O Toxin and Inhibits Its Hemolytic Effects and Cytotoxicity.Frontiers in pharmacology · 2022Article
- A pore-forming protein-induced surface-enhanced Raman spectroscopic strategy for dynamic tracing of cell membrane repair.iScience · 2021Article
- Review
- Molecular Mechanisms of Mast Cell Activation by Cholesterol-Dependent Cytolysins.Frontiers in immunology · 2021Review
- Synthesized Geopolymers Adsorb Bacterial Proteins, Toxins, and Cells.Frontiers in bioengineering and biotechnology · 2020Article
- Expansion of the Transporter-Opsin-G protein-coupled receptor superfamily with five new protein families.PloS one · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Cholesterol-dependent cytolysins (CDCs) are a large family of bacterial toxins that exhibit a dependence on the presence of membrane cholesterol in forming large pores in cell membranes. Significant changes in the three-dimensional structure of these toxins are necessary to convert the soluble monomeric protein into a membrane pore. We have determined the crystal structure of the archetypical member of the CDC family, streptolysin O (SLO), a virulence factor from Streptococcus pyogenes. The overall fold is similar to previously reported CDC structures, although the C-terminal domain is in a different orientation with respect to the rest of the molecule. Surprisingly, a signature stretch of CDC sequence called the undecapeptide motif, a key region involved in membrane recognition, adopts a very different structure in SLO to that of the well-characterized CDC perfringolysin O (PFO), although the sequences in this region are identical. An analysis reveals that, in PFO, there are complementary interactions between the motif and the rest of domain 4 that are lost in SLO. Molecular dynamics simulations suggest that the loss of a salt bridge in SLO and a cation-pi interaction are determining factors in the extended conformation of the motif, which in turn appears to result in a greater flexibility of the neighboring L1 loop that houses a cholesterol-sensing motif. These differences may explain the differing abilities of SLO and PFO to efficiently penetrate target cell membranes in the first step of toxin insertion into the membrane.
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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.