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The Gb3-enriched CD59/flotillin Plasma Membrane Domain Regulates Host Cell Invasion by Pseudomonas Aeruginosa
Annette Brandel
Sahaja Aigal
Simon Lagies
Manuel Schlimpert
Ana Valeria Meléndez Mayorga
Maokai Xu
Anika Lehmann
Daniel Hummel
Daniel Fisch
Josef Madl
Thorsten Eierhoff
Bernd Kammerer
Winfried Römer
出版
Universität
, 2021
URL
http://books.google.com.hk/books?id=7CeJzgEACAAJ&hl=&source=gbs_api
註釋
Abstract: The opportunistic pathogen Pseudomonas aeruginosa has gained precedence over the years due to its ability to develop resistance to existing antibiotics, thereby necessitating alternative strategies to understand and combat the bacterium. Our previous work identified the interaction between the bacterial lectin LecA and its host cell glycosphingolipid receptor globotriaosylceramide (Gb3) as a crucial step for the engulfment of P. aeruginosa via the lipid zipper mechanism. In this study, we define the LecA-associated host cell membrane domain by pull-down and mass spectrometry analysis. We unraveled a predilection of LecA for binding to saturated, long fatty acyl chain-containing Gb3 species in the extracellular membrane leaflet and an induction of dynamic phosphatidylinositol (3,4,5)-trisphosphate (PIP3) clusters at the intracellular leaflet co-localizing with sites of LecA binding. We found flotillins and the GPI-anchored protein CD59 not only to be an integral part of the LecA-interacting membrane domain, but also majorly influencing bacterial invasion as depletion of either of these host cell proteins resulted in about 50% reduced invasiveness of the P. aeruginosa strain PAO1. In summary, we report that the LecA-Gb3 interaction at the extracellular leaflet induces the formation of a plasma membrane domain enriched in saturated Gb3 species, CD59, PIP3 and flotillin thereby facilitating efficient uptake of PAO1