Lipid bilayer degradation induced by SARS-CoV-2 spike protein as revealed by neutron reflectometry

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 abunda...

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Autores principales: Alessandra Luchini, Samantha Micciulla, Giacomo Corucci, Krishna Chaithanya Batchu, Andreas Santamaria, Valerie Laux, Tamim Darwish, Robert A. Russell, Michel Thepaut, Isabelle Bally, Franck Fieschi, Giovanna Fragneto
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/839d4a64e2a145619d17f2cff73dae9e
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spelling oai:doaj.org-article:839d4a64e2a145619d17f2cff73dae9e2021-12-02T17:55:04ZLipid bilayer degradation induced by SARS-CoV-2 spike protein as revealed by neutron reflectometry10.1038/s41598-021-93996-x2045-2322https://doaj.org/article/839d4a64e2a145619d17f2cff73dae9e2021-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-93996-xhttps://doaj.org/toc/2045-2322Abstract 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.Alessandra LuchiniSamantha MicciullaGiacomo CorucciKrishna Chaithanya BatchuAndreas SantamariaValerie LauxTamim DarwishRobert A. RussellMichel ThepautIsabelle BallyFranck FieschiGiovanna FragnetoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Alessandra Luchini
Samantha Micciulla
Giacomo Corucci
Krishna Chaithanya Batchu
Andreas Santamaria
Valerie Laux
Tamim Darwish
Robert A. Russell
Michel Thepaut
Isabelle Bally
Franck Fieschi
Giovanna Fragneto
Lipid bilayer degradation induced by SARS-CoV-2 spike protein as revealed by neutron reflectometry
description 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.
format article
author Alessandra Luchini
Samantha Micciulla
Giacomo Corucci
Krishna Chaithanya Batchu
Andreas Santamaria
Valerie Laux
Tamim Darwish
Robert A. Russell
Michel Thepaut
Isabelle Bally
Franck Fieschi
Giovanna Fragneto
author_facet Alessandra Luchini
Samantha Micciulla
Giacomo Corucci
Krishna Chaithanya Batchu
Andreas Santamaria
Valerie Laux
Tamim Darwish
Robert A. Russell
Michel Thepaut
Isabelle Bally
Franck Fieschi
Giovanna Fragneto
author_sort Alessandra Luchini
title Lipid bilayer degradation induced by SARS-CoV-2 spike protein as revealed by neutron reflectometry
title_short Lipid bilayer degradation induced by SARS-CoV-2 spike protein as revealed by neutron reflectometry
title_full Lipid bilayer degradation induced by SARS-CoV-2 spike protein as revealed by neutron reflectometry
title_fullStr Lipid bilayer degradation induced by SARS-CoV-2 spike protein as revealed by neutron reflectometry
title_full_unstemmed Lipid bilayer degradation induced by SARS-CoV-2 spike protein as revealed by neutron reflectometry
title_sort lipid bilayer degradation induced by sars-cov-2 spike protein as revealed by neutron reflectometry
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/839d4a64e2a145619d17f2cff73dae9e
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