Lipid bilayer degradation induced by SARS-CoV-2 spike protein as revealed by neutron reflectometry
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Date
2021-07-21
Journal Title
Journal ISSN
Volume Title
Publisher
Springer Nature Limited
Abstract
SARS-CoV-2 spike proteins are responsible for the membrane fusion event, which allows the virus to enter the host cell and cause infection. This process starts with the binding of the spike extramembrane domain to the angiotensin-converting enzyme 2 (ACE2), a membrane receptor highly abundant in the lungs. In this study, the extramembrane domain of SARS-CoV-2 Spike (sSpike) was injected on model membranes formed by supported lipid bilayers in presence and absence of the soluble part of receptor ACE2 (sACE2), and the structural features were studied at sub-nanometer level by neutron reflection. In all cases the presence of the protein produced a remarkable degradation of the lipid bilayer. Indeed, both for membranes from synthetic and natural lipids, a significant reduction of the surface coverage was observed. Quartz crystal microbalance measurements showed that lipid extraction starts immediately after sSpike protein injection. All measurements indicate that the presence of proteins induces the removal of membrane lipids, both in the presence and in the absence of ACE2, suggesting that sSpike molecules strongly associate with lipids, and strip them away from the bilayer, via a non-specific interaction. A cooperative effect of sACE2 and sSpike on lipid extraction was also observed. © 2021 The Authors CC BY 4.0
Description
Keywords
Lipids, Coronaviruses, Viruses, Proteins, Neutron reflectors, Infectious diseases, Viral diseases, Lungs, Membranes
Citation
Luchini, A., Micciulla, S., Corucci, G., Batchu, K. C., Santamaria, A., Laux, V., Darwish, T., Russell, R. A., Thepaut, M., Bally, I., Fieschi, F., & Fragneto, G. (2021). Lipid bilayer degradation induced by SARS-CoV-2 spike protein as revealed by neutron reflectometry. Scientific Reports, 11(1), 14867. doi:10.1038/s41598-021-93996-x