About: Distinct conformational states of SARS-CoV-2 spike protein

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About: Distinct conformational states of SARS-CoV-2 spike protein Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Distinct conformational states of SARS-CoV-2 spike protein
Creator	Chen, Bing Xiao, Zhang, Cai, Yongfei Peng, Hanqin Rawson, Shaun Rits-Volloch, Sophia Sterling, Sarah Walsh, Richard
Source	BioRxiv; Medline
abstract	The ongoing SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) pandemic has created urgent needs for intervention strategies to control the crisis. The spike (S) protein of the virus forms a trimer and catalyzes fusion between viral and target cell membranes - the first key step of viral infection. Here we report two cryo-EM structures, both derived from a single preparation of the full-length S protein, representing the prefusion (3.1Å resolution) and postfusion (3.3Å resolution) conformations, respectively. The spontaneous structural transition to the postfusion state under mild conditions is independent of target cells. The prefusion trimer forms a tightly packed structure with three receptor-binding domains clamped down by a segment adjacent to the fusion peptide, significantly different from recently published structures of a stabilized S ectodomain trimer. The postfusion conformation is a rigid tower-like trimer, but decorated by N-linked glycans along its long axis with almost even spacing, suggesting possible involvement in a mechanism protecting the virus from host immune responses and harsh external conditions. These findings advance our understanding of how SARS-CoV-2 enters a host cell and may guide development of vaccines and therapeutics.
has issue date	2020-05-17(xsd:dateTime)
bibo:doi	10.1101/2020.05.16.099317
bibo:pmid	32511405
has license	biorxiv
sha1sum (hex)	c92ccc2c5a4844d43340d471e3b5c8bdd98f1a4f
schema:url	https://doi.org/10.1101/2020.05.16.099317
resource representing a document's title	Distinct conformational states of SARS-CoV-2 spike protein
has PubMed identifier	32511405
schema:publication	bioRxiv
resource representing a document's body	covid:c92ccc2c5a4844d43340d471e3b5c8bdd98f1a4f#body_text
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