ArticleProceedings of the National Academy of Sciences of the United States of America2011
Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.
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89 citing papers in PubMed, 163 citations in OpenAlex.
- Diversity and evolution of leukotoxin operons inmSystems · 2026Article
- The Pathogenicity Mechanisms ofInternational journal of molecular sciences · 2025Review
- Cell targeting by the bicomponent leukocidin subunit HlgB drives Staphylococcus aureus pathophysiology.The Journal of biological chemistry · 2025Article
- The virulence toolkit of Staphylococcus aureus: a comprehensive review of toxin diversity, molecular mechanisms, and clinical implications.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025Review
- 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
- Overview of Bacterial Protein Toxins from Pathogenic Bacteria: Mode of Action and Insights into Evolution.Toxins · 2024Review
- Molecular Characteristics and Pathogenicity ofInternational journal of molecular sciences · 2023Review
- Structural basis for calcium-stimulating pore formation of Vibrio α-hemolysin.Nature communications · 2023Article
- Complex Regulation of Gamma-Hemolysin Expression Impacts Staphylococcus aureus Virulence.Microbiology spectrum · 2023Article
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Gamma-Hemolysin Components: Computational Strategies for LukF-Hlg2 Dimer Reconstruction on a Model Membrane.International journal of molecular sciences · 2023Article
- Cryo-EM structure of the octameric pore of Clostridium perfringens β-toxin.EMBO reports · 2022Article
- Expression of Staphylococcal Virulence Genes In Situ in Human Skin and Soft Tissue Infections.Antibiotics (Basel, Switzerland) · 2022Article
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- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Hesperidin inhibits biofilm formation, virulence and staphyloxanthin synthesis in methicillin resistant Staphylococcus aureus by targeting SarA and CrtM: an in vitro and in silico approach.World journal of microbiology & biotechnology · 2022Article
- Correlating biological activity to thermo-structural analysis of the interaction of CTX with synthetic models of macrophage membranes.Scientific reports · 2021Article
- Pathogenicity and virulence ofVirulence · 2021Review
29 more citing papers are in PubMed but not listed here.
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10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcal γ-hemolysin is a bicomponent pore-forming toxin composed of LukF and Hlg2. These proteins are expressed as water-soluble monomers and then assemble into the oligomeric pore form on the target cell. Here, we report the crystal structure of the octameric pore form of γ-hemolysin at 2.5 Å resolution, which is the first high-resolution structure of a β-barrel transmembrane protein composed of two proteins reported to date. The octameric assembly consists of four molecules of LukF and Hlg2 located alternately in a circular pattern, which explains the biochemical data accumulated over the past two decades. The structure, in combination with the monomeric forms, demonstrates the elaborate molecular machinery involved in pore formation by two different molecules, in which interprotomer electrostatic interactions using loops connecting β2 and β3 (loop A: Asp43-Lys48 of LukF and Lys37-Lys43 of Hlg2) play pivotal roles as the structural determinants for assembly through unwinding of the N-terminal β-strands (amino-latch) of the adjacent protomer, releasing the transmembrane stem domain folded into a β-sheet in the monomer (prestem), and interaction with the adjacent protomer.
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