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
-
Omidvar, Ramin
Ayala, Yareni A.
Brandel, Annette
Hasenclever, Lukas
Helmstädter, Martin
Rohrbach, Alexander
Römer, Winfried
Madl, Josef
- DOI
-
10.1039/d0nr07726g
- URN
-
urn:nbn:de:bsz:25-freidok-1942540
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
25.03.2025, 13:51 MEZ
Datenpartner
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Omidvar, Ramin
- Ayala, Yareni A.
- Brandel, Annette
- Hasenclever, Lukas
- Helmstädter, Martin
- Rohrbach, Alexander
- Römer, Winfried
- Madl, Josef
- Universität
Entstanden
- 2021