Cell membranes are a vital part of all cells, and the lipid bilayer composed of hydrophilic heads and hydrophobic tails, provides a key defense for its cell against the environment and foreign invaders, while also responsible for signaling responses and other cell-cell interactions like gap junctions. In order to propagate itself, viruses invade and utilize its host’s own membrane against it via membrane reorganization spurred by protein binding. In particular, viral binding is known to cause "raft partitioning proteins'' to be organized around the virus. How a phase-separating vesicle organizes its domain in response to protein-binding interactions is a topic of interest. In this research, we examined the spatial organization of lipid domains at the intermembrane junction between two protein-bound lipid membranes using a model membrane reconstitution. Artificial membrane vesicles, specifically giant unilamellar vesicle (GUVs) and supported lipid bilayers (SLBs) were engineered to anchor model binding pair proteins, and were examined after establishing the intermembrane interaction with confocal laser scanning fluorescence microscopy. Results show an established relationship between the reorganization of phase-separating GUVs as a result of protein-protein interactions, specifically a strong preference for the polarization of one domain at the intermembrane junction.

Observing the spatial reorganization of lipid domains via protein-protein interactions at the intermembrane junction

ACS Spring 2022

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