ArticleProceedings of the National Academy of Sciences of the United States of America2020
Molecular mechanism of leukocidin GH-integrin CD11b/CD18 recognition and species specificity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Bacterial pore-forming toxins: mechanisms and implications for host immunity.Bioscience reports · 2026Review
- Identification and structural characterization of anthrax toxin receptor 2 as the Clostridium perfringens NetF receptor.Nature communications · 2026Article
- Article
- The Susceptibility Profiles of Human Peripheral Blood Cells toMicroorganisms · 2025Review
- Transcriptomic and Biochemical Analysis of the Antimicrobial Mechanism of Lipopeptide Iturin W againstInternational journal of molecular sciences · 2024Article
- The Relative Importance of Cytotoxins Produced by Methicillin-ResistantMicroorganisms · 2024Article
- αStructure (London, England : 1993) · 2024Article
- Overview of Bacterial Protein Toxins from Pathogenic Bacteria: Mode of Action and Insights into Evolution.Toxins · 2024Review
- αbioRxiv : the preprint server for biology · 2024Article
- Toll-like receptors and integrins crosstalk.Frontiers in immunology · 2024Review
- Draft genome sequence of Staphylococcus aureus sequence type 5 SA01 isolated from bloodstream infection and comparative analysis with reference strains.Functional & integrative genomics · 2023Article
- Cryo-EM structure of the octameric pore of Clostridium perfringens β-toxin.EMBO reports · 2022Article
- The influenza-injured lung microenvironment promotes MRSA virulence, contributing to severe secondary bacterial pneumonia.Cell reports · 2022Article
- Structural basis for non-canonical integrin engagement by Bordetella adenylate cyclase toxin.Cell reports · 2022Article
- Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Genetic variation of staphylococcal LukAB toxin determines receptor tropism.Nature microbiology · 2021Article
- Carbon Source-Dependent Reprogramming of Anaerobic Metabolism in Staphylococcus aureus.Journal of bacteriology · 2021Article
- Pore-Forming Toxins During Bacterial Infection: Molecular Mechanisms and Potential Therapeutic Targets.Drug design, development and therapy · 2021Review
- The Promiscuous Profile of Complement Receptor 3 in Ligand Binding, Immune Modulation, and Pathophysiology.Frontiers in immunology · 2021Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Host-pathogen interactions are central to understanding microbial pathogenesis. The staphylococcal pore-forming cytotoxins hijack important immune molecules but little is known about the underlying molecular mechanisms of cytotoxin-receptor interaction and host specificity. Here we report the structures of a staphylococcal pore-forming cytotoxin, leukocidin GH (LukGH), in complex with its receptor (the α-I domain of complement receptor 3, CD11b-I), both for the human and murine homologs. We observe 2 binding interfaces, on the LukG and the LukH protomers, and show that human CD11b-I induces LukGH oligomerization in solution. LukGH binds murine CD11b-I weakly and is inactive toward murine neutrophils. Using a LukGH variant engineered to bind mouse CD11b-I, we demonstrate that cytolytic activity does not only require binding but also receptor-dependent oligomerization. Our studies provide an unprecedented insight into bicomponent leukocidin-host receptor interaction, enabling the development of antitoxin approaches and improved animal models to explore these approaches.
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