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About:
A thermostable, closed, SARS-CoV-2 spike protein trimer
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covidontheweb.inria.fr
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research paper
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
title
A thermostable, closed, SARS-CoV-2 spike protein trimer
Creator
Goodfellow, Ian
Zhang, Ying
Hosmillo, Myra
Baker, Stephen
Xiong, Xiaoli
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source
BioRxiv
abstract
The spike (S) protein of SARS-CoV-2 mediates receptor binding and cell entry and is the dominant target of the immune system. S exhibits substantial conformational flexibility. It transitions from closed to open conformations to expose its receptor binding site, and subsequently from prefusion to postfusion conformations to mediate fusion of viral and cellular membranes. S protein derivatives are components of vaccine candidates and diagnostic assays, as well as tools for research into the biology and immunology of SARS-CoV-2. Here we have designed mutations in S which allow production of thermostable, crosslinked, S protein trimers that are trapped in the closed, pre-fusion, state. We have determined the structures of crosslinked and non-crosslinked proteins, identifying two distinct closed conformations of the S trimer. We demonstrate that the designed, thermostable, closed S trimer can be used in serological assays. This protein has potential applications as a reagent for serology, virology and as an immunogen.
has issue date
2020-06-17
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bibo:doi
10.1101/2020.06.15.152835
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biorxiv
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34f30726b9bc493be2c0aa03ccc269b73bd6592c
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https://doi.org/10.1101/2020.06.15.152835
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A thermostable, closed, SARS-CoV-2 spike protein trimer
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bioRxiv
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covid:34f30726b9bc493be2c0aa03ccc269b73bd6592c#body_text
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named entity 'dominant'
named entity 'cellular membranes'
named entity 'protein'
named entity 'thermostable'
named entity 'SARS-CoV-2'
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