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

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

Standort
Deutsche Nationalbibliothek Frankfurt am Main
Umfang
Online-Ressource
Sprache
Englisch
Anmerkungen
Nanoscale. - 13, 7 (2021) , 4016-4028, ISSN: 2040-3372

Ereignis
Veröffentlichung
(wo)
Freiburg
(wer)
Universität
(wann)
2021
Urheber

DOI
10.1039/d0nr07726g
URN
urn:nbn:de:bsz:25-freidok-1942540
Rechteinformation
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Letzte Aktualisierung
25.03.2025, 13:51 MEZ

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  • 2021

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