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Omidvar, Ramin [VerfasserIn]; Ayala, Yareni A. [VerfasserIn]; Brandel, Annette [VerfasserIn]; Hasenclever, Lukas [VerfasserIn]; Helmstädter, Martin [VerfasserIn]; Rohrbach, Alexander [VerfasserIn]; Römer, Winfried [VerfasserIn]; Madl, Josef [VerfasserIn]

Quantification of nanoscale forces in lectin-mediated bacterial attachment and uptake into giant liposomes

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  • Medientyp: E-Book; Sonderdruck
  • Titel: Quantification of nanoscale forces in lectin-mediated bacterial attachment and uptake into giant liposomes
  • Beteiligte: Omidvar, Ramin [VerfasserIn]; Ayala, Yareni A. [VerfasserIn]; Brandel, Annette [VerfasserIn]; Hasenclever, Lukas [VerfasserIn]; Helmstädter, Martin [VerfasserIn]; Rohrbach, Alexander [VerfasserIn]; Römer, Winfried [VerfasserIn]; Madl, Josef [VerfasserIn]
  • Erschienen: Cambridge: Royal Society of Chemistry, 2021
  • Erschienen in: Nanoscale ; 13, 7 (2021), 4016-4028
  • Umfang: 1 Online-Ressource (14 Seiten); Illustrationen, Diagramme; Supplementary Files
  • Sprache: Englisch
  • DOI: 10.1039/d0nr07726g
  • ISSN: 2040-3372
  • Identifikator:
  • Entstehung:
  • Anmerkungen:
  • Beschreibung: Abstract: Interactions of the bacterial lectin LecA with the host cells glycosphingolipid Gb3 have been shown to be crucial for the cellular uptake of the bacterium Pseudomonas aeruginosa. LecA-induced Gb3 clustering, referred to as lipid zipper mechanism, leads to full membrane engulfment of the bacterium. Here, we aim for a nanoscale force characterization of this mechanism using two complementary force probing techniques, atomic force microscopy (AFM) and optical tweezers (OT). The LecA–Gb3 interactions are reconstituted using giant unilamellar vesicles (GUVs), a well-controlled minimal system mimicking the plasma membrane and nanoscale forces between either bacteria (PAO1 wild-type and LecA-deletion mutant strains) or LecA-coated probes (as minimal, synthetic bacterial model) and vesicles are measured. LecA–Gb3 interactions strengthen the bacterial attachment to the membrane (1.5–8-fold) depending on the membrane tension and the applied technique. Moreover, significantly less energy (reduction up to 80%) is required for the full uptake of LecA-coated beads into Gb3-functionalized vesicles. This quantitative approach highlights that lectin–glycolipid interactions provide adequate forces and energies to drive bacterial attachment and uptake
  • Zugangsstatus: Freier Zugang