Minimal system for assembly of SARS-CoV-2 virus like particles

Minimal system for assembly of SARS-CoV-2 virus like particles

Abstract SARS-CoV-2 virus is the causative agent of COVID-19. Here we demonstrate that non-infectious SARS-CoV-2 virus like particles (VLPs) can be assembled by co-expressing the viral proteins S, M and E in mammalian cells. The assembled SARS-CoV-2 VLPs possess S protein spikes on particle exterior...

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Main Authors: Heather Swann, Abhimanyu Sharma, Benjamin Preece, Abby Peterson, Crystal Eldridge, David M. Belnap, Michael Vershinin, Saveez Saffarian
Format: Article
Language:English
Published: Nature Publishing Group 2020-12-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-020-78656-w
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spelling doaj-c04addeea9b342c79dfabdf0aada97952020-12-20T12:27:52ZengNature Publishing GroupScientific Reports2045-23222020-12-011011510.1038/s41598-020-78656-wMinimal system for assembly of SARS-CoV-2 virus like particlesHeather Swann0Abhimanyu Sharma1Benjamin Preece2Abby Peterson3Crystal Eldridge4David M. Belnap5Michael Vershinin6Saveez Saffarian7Center for Cell and Genome Science, University of UtahDepartment of Physics and Astronomy, University of UtahCenter for Cell and Genome Science, University of UtahCenter for Cell and Genome Science, University of UtahCenter for Cell and Genome Science, University of UtahSchool of Biological Sciences, University of UtahCenter for Cell and Genome Science, University of UtahCenter for Cell and Genome Science, University of UtahAbstract SARS-CoV-2 virus is the causative agent of COVID-19. Here we demonstrate that non-infectious SARS-CoV-2 virus like particles (VLPs) can be assembled by co-expressing the viral proteins S, M and E in mammalian cells. The assembled SARS-CoV-2 VLPs possess S protein spikes on particle exterior, making them ideal for vaccine development. The particles range in shape from spherical to elongated with a characteristic size of 129 ± 32 nm. We further show that SARS-CoV-2 VLPs dried in ambient conditions can retain their structural integrity upon repeated scans with Atomic Force Microscopy up to a peak force of 1 nN.https://doi.org/10.1038/s41598-020-78656-w
collection DOAJ
language English
format Article
sources DOAJ
author Heather Swann
Abhimanyu Sharma
Benjamin Preece
Abby Peterson
Crystal Eldridge
David M. Belnap
Michael Vershinin
Saveez Saffarian
spellingShingle Heather Swann
Abhimanyu Sharma
Benjamin Preece
Abby Peterson
Crystal Eldridge
David M. Belnap
Michael Vershinin
Saveez Saffarian
Minimal system for assembly of SARS-CoV-2 virus like particles
Scientific Reports
author_facet Heather Swann
Abhimanyu Sharma
Benjamin Preece
Abby Peterson
Crystal Eldridge
David M. Belnap
Michael Vershinin
Saveez Saffarian
author_sort Heather Swann
title Minimal system for assembly of SARS-CoV-2 virus like particles
title_short Minimal system for assembly of SARS-CoV-2 virus like particles
title_full Minimal system for assembly of SARS-CoV-2 virus like particles
title_fullStr Minimal system for assembly of SARS-CoV-2 virus like particles
title_full_unstemmed Minimal system for assembly of SARS-CoV-2 virus like particles
title_sort minimal system for assembly of sars-cov-2 virus like particles
publisher Nature Publishing Group
series Scientific Reports
issn 2045-2322
publishDate 2020-12-01
description Abstract SARS-CoV-2 virus is the causative agent of COVID-19. Here we demonstrate that non-infectious SARS-CoV-2 virus like particles (VLPs) can be assembled by co-expressing the viral proteins S, M and E in mammalian cells. The assembled SARS-CoV-2 VLPs possess S protein spikes on particle exterior, making them ideal for vaccine development. The particles range in shape from spherical to elongated with a characteristic size of 129 ± 32 nm. We further show that SARS-CoV-2 VLPs dried in ambient conditions can retain their structural integrity upon repeated scans with Atomic Force Microscopy up to a peak force of 1 nN.
url https://doi.org/10.1038/s41598-020-78656-w
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AT crystaleldridge minimalsystemforassemblyofsarscov2viruslikeparticles
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