返回Google圖書搜尋

Quantification of Nanoscale Forces in Lectin-mediated Bacterial Attachment and Uptake Into Giant Liposomes

Ramin OmidvarYareni A. AyalaAnnette BrandelLukas HasencleverMartin HelmstädterAlexander RohrbachWinfried RömerJosef Madl

出版	Universität, 2021
URL	http://books.google.com.hk/books?id=gu57zgEACAAJ&hl=&source=gbs_api

註釋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