Study of the Interaction of the S-Protein of SARS-CoV-2 with Isolated Lipid Model Membranes

Abstract

The interaction of the ectodomain of the human coronavirus spike protein with the phospholipid monolayers formed on the aqueous subphase surface has been investigated. The changes in the molecular organization of monolayers of two neutral phospholipids—dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylethanolamine—after the injection of a protein solution underneath the monolayer have been analyzed. Experiments were performed with a recombinant ectodomain of the S-protein, expressed in a CHO-K1 cell strain. Electron microscopy data showed that the protein is trimerized. Grazing incidence diffraction measurements were performed to study the influence of the trimer ectodomain of the S-protein on the structure of the dipalmitoylphosphatidylcholine monolayer. It is found that protein injection under the monolayer does not induce disturbance of the monolayer crystal structure. The experimental results obtained in X-ray studies and compression isotherm measurements indicate that the interaction with the S-protein does not result in destabilization of the monolayer for both phospholipids.