Increased elastase sensitivity and decreased intramolecular interactions in the more transmissible 501Y.V1 and 501Y.V2 SARS-CoV-2 variants' spike protein-an in silico analysis.

Pokhrel, S; Kraemer, BR; Lee, L; Samardzic, K; Mochly-Rosen, D

Increased elastase sensitivity and decreased intramolecular interactions in the more transmissible 501Y.V1 and 501Y.V2 SARS-CoV-2 variants' spike protein-an in silico analysis.

Pokhrel, S Kraemer, BR Lee, L Samardzic, K

Mochly-Rosen, D

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Publisher:: PUBLIC LIBRARY SCIENCE
Publication Type:: Journal Article
Citation:: PLoS One, 2021, 16, (5), pp. 1-14
Issue Date:: 2021

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Field	Value	Language
dc.contributor.author	Pokhrel, S
dc.contributor.author	Kraemer, BR
dc.contributor.author	Lee, L
dc.contributor.author	Samardzic, K https://orcid.org/0000-0001-6177-5561
dc.contributor.author	Mochly-Rosen, D
dc.date.accessioned	2022-04-26T04:18:21Z
dc.date.available	2021-04-26
dc.date.available	2022-04-26T04:18:21Z
dc.date.issued	2021
dc.identifier.citation	PLoS One, 2021, 16, (5), pp. 1-14
dc.identifier.issn	1932-6203
dc.identifier.issn	1932-6203
dc.identifier.uri	http://hdl.handle.net/10453/156604
dc.description.abstract	Two SARS-CoV-2 variants of concern showing increased transmissibility relative to the Wuhan virus have recently been identified. Although neither variant appears to cause more severe illness nor increased risk of death, the faster spread of the virus is a major threat. Using computational tools, we found that the new SARS-CoV-2 variants may acquire an increased transmissibility by increasing the propensity of its spike protein to expose the receptor binding domain via proteolysis, perhaps by neutrophil elastase and/or via reduced intramolecular interactions that contribute to the stability of the closed conformation of spike protein. This information leads to the identification of potential treatments to avert the imminent threat of these more transmittable SARS-CoV-2 variants.
dc.format	Electronic-eCollection
dc.language	eng
dc.publisher	PUBLIC LIBRARY SCIENCE
dc.relation.ispartof	PLoS One
dc.relation.isbasedon	10.1371/journal.pone.0251426
dc.rights	info:eu-repo/semantics/openAccess
dc.subject.classification	General Science & Technology
dc.subject.mesh	Amino Acid Sequence
dc.subject.mesh	Angiotensin-Converting Enzyme 2
dc.subject.mesh	Antibodies, Neutralizing
dc.subject.mesh	COVID-19
dc.subject.mesh	Humans
dc.subject.mesh	Molecular Dynamics Simulation
dc.subject.mesh	Mutation
dc.subject.mesh	Neutrophils
dc.subject.mesh	Pancreatic Elastase
dc.subject.mesh	Protein Binding
dc.subject.mesh	Protein Stability
dc.subject.mesh	Protein Structure, Tertiary
dc.subject.mesh	SARS-CoV-2
dc.subject.mesh	Sequence Alignment
dc.subject.mesh	Spike Glycoprotein, Coronavirus
dc.subject.mesh	Amino Acid Sequence
dc.subject.mesh	Angiotensin-Converting Enzyme 2
dc.subject.mesh	Antibodies, Neutralizing
dc.subject.mesh	COVID-19
dc.subject.mesh	Humans
dc.subject.mesh	Molecular Dynamics Simulation
dc.subject.mesh	Mutation
dc.subject.mesh	Neutrophils
dc.subject.mesh	Pancreatic Elastase
dc.subject.mesh	Protein Binding
dc.subject.mesh	Protein Stability
dc.subject.mesh	Protein Structure, Tertiary
dc.subject.mesh	SARS-CoV-2
dc.subject.mesh	Sequence Alignment
dc.subject.mesh	Spike Glycoprotein, Coronavirus
dc.subject.mesh	Neutrophils
dc.subject.mesh	Humans
dc.subject.mesh	Pancreatic Elastase
dc.subject.mesh	Sequence Alignment
dc.subject.mesh	Amino Acid Sequence
dc.subject.mesh	Protein Structure, Tertiary
dc.subject.mesh	Protein Binding
dc.subject.mesh	Mutation
dc.subject.mesh	Protein Stability
dc.subject.mesh	Molecular Dynamics Simulation
dc.subject.mesh	Antibodies, Neutralizing
dc.subject.mesh	Spike Glycoprotein, Coronavirus
dc.subject.mesh	COVID-19
dc.subject.mesh	Angiotensin-Converting Enzyme 2
dc.subject.mesh	SARS-CoV-2
dc.title	Increased elastase sensitivity and decreased intramolecular interactions in the more transmissible 501Y.V1 and 501Y.V2 SARS-CoV-2 variants' spike protein-an in silico analysis.
dc.type	Journal Article
utslib.citation.volume	16
utslib.location.activity	United States
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
utslib.copyright.status	open_access	*
pubs.consider-herdc	false
dc.date.updated	2022-04-26T04:18:15Z
pubs.issue	5
pubs.publication-status	Published
pubs.volume	16
utslib.citation.issue	5

Abstract:

Two SARS-CoV-2 variants of concern showing increased transmissibility relative to the Wuhan virus have recently been identified. Although neither variant appears to cause more severe illness nor increased risk of death, the faster spread of the virus is a major threat. Using computational tools, we found that the new SARS-CoV-2 variants may acquire an increased transmissibility by increasing the propensity of its spike protein to expose the receptor binding domain via proteolysis, perhaps by neutrophil elastase and/or via reduced intramolecular interactions that contribute to the stability of the closed conformation of spike protein. This information leads to the identification of potential treatments to avert the imminent threat of these more transmittable SARS-CoV-2 variants.

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http://hdl.handle.net/10453/156604