About: Structural basis for human coronavirus attachment to sialic acid receptors

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About: Structural basis for human coronavirus attachment to sialic acid receptors 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	Structural basis for human coronavirus attachment to sialic acid receptors
Creator	Bosch, Berend-Jan Veesler, David Walls, Alexandra Boons, Geert-Jan Li, Zeshi Wang, Chunyan Lang, Yifei Koerhuis, Danielle De Groot, Raoul Rey, Félix Tortorici, M
Source	Medline; PMC
abstract	Coronaviruses cause respiratory tract infections in humans and outbreaks of deadly pneumonia worldwide. Infections are initiated by the transmembrane spike (S) glycoprotein, which binds to host receptors and fuses the viral and cellular membranes. To understand the molecular basis of coronavirus attachment to oligosaccharide receptors, we determined cryo-EM structures of coronavirus OC43 S glycoprotein trimer in isolation and in complex with a 9-O-acetylated sialic acid. We demonstrate that the ligand binds with fast kinetics to a surface-exposed groove and interactions at the identified site are essential for S-mediated viral entry into host cells, but free monosaccharide did not trigger fusogenic conformational changes. The receptor-interacting site is conserved in all coronavirus S glycoproteins that engage 9-O-acetyl-sialogycans, with an architecture similar to the ligand-binding pockets of coronavirus hemagglutinin esterases and influenza virus C/D hemagglutinin-esterase-fusion glycoproteins. Our results demonstrate these viruses evolved similar strategies to engage sialoglycans at the surface of target cells.
has issue date	2019-06-03(xsd:dateTime)
bibo:doi	10.1038/s41594-019-0233-y
bibo:pmid	31160783
has license	no-cc
sha1sum (hex)	e4ce8d53c967210c83f5b7d7b0a702fb2677c9db
schema:url	https://doi.org/10.1038/s41594-019-0233-y
resource representing a document's title	Structural basis for human coronavirus attachment to sialic acid receptors
has PubMed Central identifier	PMC6554059
has PubMed identifier	31160783
schema:publication	Nat Struct Mol Biol
resource representing a document's body	covid:e4ce8d53c967210c83f5b7d7b0a702fb2677c9db#body_text
is schema:about of	named entity 'site' named entity 'transmembrane' named entity 'worldwide' named entity 'virus' named entity 'viral' named entity 'ENGAGE' named entity 'VIRAL ENTRY' named entity 'GLYCOPROTEIN' named entity 'HEMAGGLUTININ' named entity 'groove' named entity 'coronavirus' named entity 'complex' named entity 'outbreaks' named entity 'glycoprotein' named entity 'basis' named entity 'conserved' named entity 'deadly' named entity 'cells' named entity 'viruses' named entity 'transmembrane' named entity 'molecular basis' named entity 'receptor' named entity 'coronavirus' named entity 'OC43' named entity 'fusogenic' named entity 'esterases' named entity 'cellular membranes' named entity 'viruses' named entity 'Coronaviruses' named entity 'sialic acid' named entity 'structures' named entity 'glycoside' named entity '4a-c' named entity 'hydrogen bond' named entity 'wild-type' named entity 'hydrophobic' named entity 'protein' named entity 'rat' named entity 'hemagglutinin' named entity 'recombinantly' named entity 'HCoV-OC43' named entity 'young children' named entity 'HCoV-229E' named entity 'Sialic acids' named entity 'neuraminic acid' named entity 'hydrogen bond' named entity '2a-c' named entity 'ligands' named entity 'decoy receptors' named entity 'ligand' named entity 'influenza' named entity 'fusogenic' named entity 'HCoV-HKU1' named entity 'coronaviruses' named entity 'HCoV-OC43' named entity 'hemagglutination' named entity 'coronaviruses' named entity 'HCoV-OC43' named entity 'HCoV-OC43' named entity 'sialic acid' named entity 'critical role' named entity 'HCoV-HKU1' named entity 'hemagglutinins' named entity 'HCoV-HKU1' named entity 'hemagglutinin-esterase' named entity 'binding site' named entity 'porcine' named entity 'cryo-EM' named entity 'biochemical' named entity 'fatality rate' named entity 'influenza'

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