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Updated: May 20, 2025

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
Published on: January 11, 2017
Optimal functioning of the Lpt bridge depends on a ternary complex between the lipocalin YedD and the LptDE
Alexandra Gennaris1, Van Son Nguyen2, Laurie Thouvenel1
1WELBIO Department, WEL Research Institute, Avenue Pasteur, 6, 1300 Wavre, Belgium; de Duve Institute, Université catholique de Louvain (UCLouvain), Avenue Hippocrate 75, 1200 Brussels, Belgium.
Abstract:
The outer membrane is an efficient permeability barrier that protects gram-negative bacteria against external assaults, including many antibiotics. The unique permeability features of the outer membrane are due to the presence of lipopolysaccharide (LPS) molecules in its outer leaflet. LPS transport relies on the essential lipopolysaccharide transport (Lpt) pathway, which forms a bridge from the inner to the outer membrane. The LptDE translocon inserts LPS into the outer leaflet. Here, we identify the lipocalin YedD as a component of the translocon. Cryoelectron microscopy of the YedD-LptDE complex reveals that YedD binds LptD at a critical interface between its β-barrel and periplasmic β-taco domain. The YedD-LptDE complex is functionally relevant: under conditions where the connectivity of the β-taco and Lpt bridge is compromised, the absence of YedD decreases cell viability and causes LPS accumulation in the inner membrane. Our findings establish YedD as an Lpt component required for optimal LPS transport.
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