ArticlePloS one2014
Residues essential for Panton-Valentine leukocidin S component binding to its cell receptor suggest both plasticity and adaptability in its interaction surface.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Cell targeting by the bicomponent leukocidin subunit HlgB drives Staphylococcus aureus pathophysiology.The Journal of biological chemistry · 2025Article
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- Development of Combination Vaccine Conferring Optimal Protection against Six Pore-Forming Toxins of Staphylococcus aureus.Infection and immunity · 2021Article
- Identification of a domain critical forThe Journal of biological chemistry · 2020Article
- Article
- Unbiased Identification of Immunogenic Staphylococcus aureus Leukotoxin B-Cell Epitopes.Infection and immunity · 2020Article
- Staphylococcus aureus toxin LukSF dissociates from its membrane receptor target to enable renewed ligand sequestration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Leukocidins: staphylococcal bi-component pore-forming toxins find their receptors.Nature reviews. Microbiology · 2017Review
- Article
- Crystal structures of the components of the Staphylococcus aureus leukotoxin ED.Acta crystallographica. Section D, Structural biology · 2016Article
- The Relationship between Glycan Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-forming Toxin.The Journal of biological chemistry · 2015Article
- The staphylococcal toxins γ-haemolysin AB and CB differentially target phagocytes by employing specific chemokine receptors.Nature communications · 2014Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Panton-Valentine leukocidin (PVL), a bicomponent staphylococcal leukotoxin, is involved in the poor prognosis of necrotizing pneumonia. The present study aimed to elucidate the binding mechanism of PVL and in particular its cell-binding domain. The class S component of PVL, LukS-PV, is known to ensure cell targeting and exhibits the highest affinity for the neutrophil membrane (Kd∼10(-10) M) compared to the class F component of PVL, LukF-PV (Kd∼10(-9) M). Alanine scanning mutagenesis was used to identify the residues involved in LukS-PV binding to the neutrophil surface. Nineteen single alanine mutations were performed in the rim domain previously described as implicated in cell membrane interactions. Positions were chosen in order to replace polar or exposed charged residues and according to conservation between leukotoxin class S components. Characterization studies enabled to identify a cluster of residues essential for LukS-PV binding, localized on two loops of the rim domain. The mutations R73A, Y184A, T244A, H245A and Y250A led to dramatically reduced binding affinities for both human leukocytes and undifferentiated U937 cells expressing the C5a receptor. The three-dimensional structure of five of the mutants was determined using X-ray crystallography. Structure analysis identified residues Y184 and Y250 as crucial in providing structural flexibility in the receptor-binding domain of LukS-PV.
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