ArticleThe Biochemical journal2006
Engineered covalent leucotoxin heterodimers form functional pores: insights into S-F interactions.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Panton-Valentine Leucocidin of Staphylococcus aureus Induces Oxidative Stress and Neurotransmitter Imbalance in a Retinal Explant Model.Investigative ophthalmology & visual science · 2021Article
- Staphylococcus aureus pore-forming toxins: The interface of pathogen and host complexity.Seminars in cell & developmental biology · 2017Review
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- Article
- The bicomponent pore-forming leucocidins of Staphylococcus aureus.Microbiology and molecular biology reviews : MMBR · 2014Review
- Staphylococcal bicomponent pore-forming toxins: targets for prophylaxis and immunotherapy.Toxins · 2014Review
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- Crystallization and preliminary crystallographic studies of both components of the staphylococcal LukE-LukD leukotoxin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- 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
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- Distinction between pore assembly by staphylococcal alpha-toxin versus leukotoxins.Journal of biomedicine & biotechnology · 2007Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The staphylococcal alpha-toxin and bipartite leucotoxins belong to a single family of pore-forming toxins that are rich in beta-strands, although the stoichiometry and electrophysiological characteristics of their pores are different. The different known structures show a common beta-sandwich domain that plays a key role in subunit-subunit interactions, which could be targeted to inhibit oligomerization of these toxins. We used several cysteine mutants of both HlgA (gamma-haemolysin A) and HlgB (gamma-haemolysin B) to challenge 20 heterodimers linked by disulphide bridges. A new strategy was developed in order to obtain a good yield for S-S bond formation and dimer stabilization. Functions of the pores formed by 14 purified dimers were investigated on model membranes, i.e. planar lipid bilayers and large unilamellar vesicles, and on target cells, i.e. rabbit and human red blood cells and polymorphonuclear neutrophils. We observed that dimers HlgA T28C-HlgB N156C and HlgA T21C-HlgB T157C form pores with similar characteristics as the wild-type toxin, thus suggesting that the mutated residues are facing one another, allowing pore formation. Our results also confirm the octameric stoichiometry of the leucotoxin pores, as well as the parity of the two monomers in the pore. Correctly assembled heterodimers thus constitute the minimal functional unit of leucotoxins. We propose amino acids involved in interactions at one of the two interfaces for an assembled leucotoxin.
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