About: Prefusion structure of a human coronavirus spike protein

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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	Prefusion structure of a human coronavirus spike protein
Creator	Pallesen, Jesper Wang, Nianshuang Corbett, Kizzmekia Cottrell, Christopher Graham, Barney Kirchdoerfer, Robert Mclellan, Jason Ward, Andrew Turner, L Yassine, M
topic	covid:af027d237d28a214db31b89c67047d49cf6e4a5b#this
Source	Medline; PMC
abstract	HKU1 is a human betacoronavirus that causes mild yet prevalent respiratory disease(1) and is related to the zoonotic SARS(2) and MERS(3) betacoronaviruses that have high fatality rates and pandemic potential. Cell tropism and host range is determined in part by the coronavirus spike (S) protein(4), which binds cellular receptors and mediates membrane fusion. As the largest known class I fusion protein, its size and extensive glycosylation have hindered structural studies of the full ectodomain, thus preventing a molecular understanding of its function and limiting development of effective interventions. Here we present the 4.0 Å resolution structure of the trimeric HKU1 S protein determined using single-particle cryo-electron microscopy. In the prefusion conformation, the receptor-binding subunits, S1, rest atop the fusion-mediating subunits, S2, preventing their conformational rearrangement. Surprisingly, the S1 C-terminal domains are interdigitated and form extensive quaternary interactions that occlude surfaces known to bind protein receptors in other coronaviruses. These features, along with the location of the two protease sites known to be important for coronavirus entry, provide a structural basis to support a model of membrane fusion mediated by progressive S protein destabilization through receptor binding and proteolytic cleavage. Additionally, these studies should serve as a foundation for the structure-based design of betacoronavirus vaccine immunogens.
has issue date	2016-03-01(xsd:dateTime)
bibo:doi	10.1038/nature17200
bibo:pmid	26935699
has license	bronze-oa
sha1sum (hex)	af027d237d28a214db31b89c67047d49cf6e4a5b
schema:url	https://doi.org/10.1038/nature17200
resource representing a document's title	Prefusion structure of a human coronavirus spike protein
has PubMed Central identifier	PMC4860016
has PubMed identifier	26935699
schema:publication	Nature
resource representing a document's body	covid:af027d237d28a214db31b89c67047d49cf6e4a5b#body_text
is http://vocab.deri.ie/void#inDataset of	https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/af027d237d28a214db31b89c67047d49cf6e4a5b
is schema:about of	named entity 'STRUCTURE' named entity 'hindered' named entity 'subunits' named entity 'trimeric' named entity 'potential' named entity 'location' named entity 'occlude' named entity 'betacoronavirus' named entity 'coronavirus' named entity 'VACCINE' named entity 'POTENTIAL' named entity 'PROTEOLYTIC' named entity 'SPIKE' named entity 'RECEPTOR BINDING' named entity 'SPIKE PROTEIN' named entity 'RESPIRATORY DISEASE' named entity 'CORONAVIRUS' named entity 'FUSION PROTEIN' named entity 'FORM' named entity 'PANDEMIC' named entity 'FUNCTION' named entity 'BINDING' named entity 'EFFECTIVE INTERVENTIONS' named entity 'PROVIDE' named entity 'IMMUNOGENS' named entity 'FOUNDATION' named entity 'CRYO-ELECTRON MICROSCOPY' named entity 'THESE' named entity 'PROTEIN DESTABILIZATION' named entity 'FEATURES' named entity 'BIND' named entity 'REST' named entity 'PREVENTING' named entity '28S' named entity 'RECEPTOR' named entity 'BASED' named entity 'MODEL OF' named entity 'S PROTEIN' named entity 'CORONAVIRUSES' named entity 'STRUCTURAL' named entity 'LARGEST' named entity 'RESOLUTION' named entity 'ENTRY' named entity 'HUMAN' named entity 'PROTEIN RECEPTORS' named entity 'EXTENSIVE' named entity 'STUDIES' named entity 'USING' named entity 'LIMITING' named entity 'MOLECULAR' named entity 'DETERMINED' named entity 'CAUSES' named entity 'HOST RANGE' named entity 'UNDERSTANDING' named entity 'CELL' named entity 'MEDIATES' named entity 'IS A' named entity 'PROGRESSIVE' named entity 'ECTODOMAIN' named entity 'TO SUPPORT' named entity 'STRUCTURE' named entity 'CLASS I' named entity 'HERE' named entity 'BINDS' named entity 'SIZE' named entity 'THEIR' named entity 'ITS' named entity 'SERVE' named entity 'MEDIATED' named entity 'HUMAN CORONAVIRUS'

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