About: Incorporation of Spike and Membrane Glycoproteins into Coronavirus Virions

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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	Incorporation of Spike and Membrane Glycoproteins into Coronavirus Virions
Creator	Ujike, Makoto Liu, Shan-Lu Taguchi, Fumihiro Johnson, Marc
Source	Medline; PMC
abstract	The envelopes of coronaviruses (CoVs) contain primarily three proteins; the two major glycoproteins spike (S) and membrane (M), and envelope (E), a non-glycosylated protein. Unlike other enveloped viruses, CoVs bud and assemble at the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC). For efficient virion assembly, these proteins must be targeted to the budding site and to interact with each other or the ribonucleoprotein. Thus, the efficient incorporation of viral envelope proteins into CoV virions depends on protein trafficking and protein–protein interactions near the ERGIC. The goal of this review is to summarize recent findings on the mechanism of incorporation of the M and S glycoproteins into the CoV virion, focusing on protein trafficking and protein–protein interactions.
has issue date	2015-04-03(xsd:dateTime)
bibo:doi	10.3390/v7041700
bibo:pmid	25855243
has license	cc-by
sha1sum (hex)	379317c0c8b61dd88b6faa235b21dd861436edcf
schema:url	https://doi.org/10.3390/v7041700
resource representing a document's title	Incorporation of Spike and Membrane Glycoproteins into Coronavirus Virions
has PubMed Central identifier	PMC4411675
has PubMed identifier	25855243
schema:publication	Viruses
resource representing a document's body	covid:379317c0c8b61dd88b6faa235b21dd861436edcf#body_text
is schema:about of	named entity 'CORONAVIRUS' named entity 'MECHANISM' named entity 'MAJOR' named entity 'PROTEIN TRAFFICKING' named entity 'TARGETED' named entity 'INTERMEDIATE' named entity '28S' named entity 'ASSEMBLE' named entity 'MEMBRANE' named entity 'VIRUSES' named entity 'VIRION ASSEMBLY' named entity 'SITE' named entity 'NON-' named entity 'THESE' named entity 'BUD' named entity 'EFFICIENT' named entity 'MEMBRANE GLYCOPROTEINS' named entity 'NEAR' named entity 'VIRION' named entity 'TO INTERACT WITH' named entity 'GLYCOSYLATED PROTEIN' named entity 'SPIKE' named entity 'VIRIONS' named entity 'CONTAIN' named entity 'FOCUSING' named entity 'VIRIONS' named entity 'PROTEIN-PROTEIN INTERACTIONS' named entity 'COMPARTMENT' named entity 'REVIEW' named entity 'GLYCOPROTEINS' named entity 'ERGIC' named entity 'SPIKE' named entity 'BUDDING' named entity 'CORONAVIRUSES' named entity 'GOAL' named entity 'RECENT' named entity 'COVS' named entity 'PROTEINS' named entity 'ENVELOPE' named entity 'VIRAL ENVELOPE PROTEINS' named entity 'GOLGI' named entity 'ENDOPLASMIC RETICULUM' named entity 'RIBONUCLEOPROTEIN' named entity 'FINDINGS' named entity 'virions' named entity 'protein' named entity 'Virions' named entity 'Membrane Glycoproteins' named entity 'gastrointestinal' named entity 'ectodomain' named entity 'phosphorylation' named entity 'IBV' named entity 'protein trafficking' named entity 'endocytosis' named entity 'VLP' named entity 'cell surface' named entity 'envelope proteins' named entity 'cysteine' named entity 'intracellular retention' named entity 'cellular machinery' named entity 'MHV' named entity 'open reading frames' named entity 'lipid bilayer' named entity 'nucleocapsid' named entity 'palmitic acids' named entity 'BCoV' named entity 'envelope proteins' named entity 'virions' named entity 'virion' named entity 'protein complex' named entity 'protein' named entity 'virion' named entity 'amino acid sequence' named entity 'protein' named entity 'epitope' named entity 'Golgi' named entity 'M proteins' named entity 'virion'

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