About: Palmitoylation of the cysteine-rich endodomain of the SARS–coronavirus spike glycoprotein is important for spike-mediated cell fusion

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About: Palmitoylation of the cysteine-rich endodomain of the SARS–coronavirus spike glycoprotein is important for spike-mediated cell fusion Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Palmitoylation of the cysteine-rich endodomain of the SARS–coronavirus spike glycoprotein is important for spike-mediated cell fusion
Creator	Farzan, Michael Colgrove, Robin Iyer, Arun Knipe, David Chouljenko, Vladimir Kousoulas, K Petit, Chad
Source	Elsevier; Medline; PMC
abstract	Abstract The SARS–coronavirus (SARS–CoV) is the etiological agent of the severe acute respiratory syndrome (SARS). The SARS–CoV spike (S) glycoprotein mediates membrane fusion events during virus entry and virus-induced cell-to-cell fusion. The cytoplasmic portion of the S glycoprotein contains four cysteine-rich amino acid clusters. Individual cysteine clusters were altered via cysteine-to-alanine amino acid replacement and the modified S glycoproteins were tested for their transport to cell-surfaces and ability to cause cell fusion in transient transfection assays. Mutagenesis of the cysteine cluster I, located immediately proximal to the predicted transmembrane, domain did not appreciably reduce cell-surface expression, although S-mediated cell fusion was reduced by more than 50% in comparison to the wild-type S. Similarly, mutagenesis of the cysteine cluster II located adjacent to cluster I reduced S-mediated cell fusion by more than 60% compared to the wild-type S, while cell-surface expression was reduced by less than 20%. Mutagenesis of cysteine clusters III and IV did not appreciably affect S cell-surface expression or S-mediated cell fusion. The wild-type S was palmitoylated as evidenced by the efficient incorporation of 3H-palmitic acid in wild-type S molecules. S glycoprotein palmitoylation was significantly reduced for mutant glycoproteins having cluster I and II cysteine changes, but was largely unaffected for cysteine cluster III and IV mutants. These results show that the S cytoplasmic domain is palmitoylated and that palmitoylation of the membrane proximal cysteine clusters I and II may be important for S-mediated cell fusion.
has issue date	2007-04-10(xsd:dateTime)
bibo:doi	10.1016/j.virol.2006.10.034
bibo:pmid	17134730
has license	els-covid
sha1sum (hex)	6bf32d3df398fe49d4798994fa96b2463a208ce5
schema:url	https://doi.org/10.1016/j.virol.2006.10.034
resource representing a document's title	Palmitoylation of the cysteine-rich endodomain of the SARS–coronavirus spike glycoprotein is important for spike-mediated cell fusion
has PubMed Central identifier	PMC7103323
has PubMed identifier	17134730
schema:publication	Virology
resource representing a document's body	covid:6bf32d3df398fe49d4798994fa96b2463a208ce5#body_text
is schema:about of	named entity 'RICH' named entity 'SARS' named entity 'TESTED FOR' named entity 'TRANSMEMBRANE' named entity 'PROXIMAL' named entity 'MEMBRANE FUSION' named entity 'THEIR' named entity 'PALMITOYLATION' named entity '3 H' named entity 'CELL' named entity 'ALTERED' named entity 'CORONAVIRUS' named entity 'UNAFFECTED' named entity 'CAUSE' named entity 'RESULTS' named entity 'REDUCED' named entity 'TRANSIENT TRANSFECTION' named entity 'DID' named entity 'PALMITOYLATED' named entity 'MEDIATES' named entity 'INDUCED' named entity 'IMPORTANT' named entity 'CYTOPLASMIC DOMAIN' named entity 'CYSTEINE' named entity 'SARS' named entity '50%' named entity 'DOMAIN' named entity 'ALANINE' named entity 'MUTANT' named entity 'EXPRESSION' named entity 'CONTAINS' named entity 'MOLECULES' named entity 'CLUSTER' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME' named entity 'PROXIMAL TO' named entity 'MUTAGENESIS' named entity 'LARGELY' named entity '28S' named entity 'IMPORTANT' named entity 'SURFACES' named entity 'VIRUS' named entity 'MEDIATED' named entity 'CYTOPLASMIC' named entity 'IMMEDIATELY' named entity 'III' named entity 'EFFICIENT' named entity 'CELL FUSION' named entity 'PALMITIC ACID' named entity 'RICH' named entity 'SARS-COV' named entity 'INDIVIDUAL' named entity 'MORE THAN' named entity 'MORE THAN 50' named entity 'AGENT' named entity 'PALMITOYLATION' named entity 'CELL FUSION' named entity 'CYSTEINE' named entity 'GLYCOPROTEINS' named entity 'BUT' named entity 'MEMBRANE' named entity 'ADJACENT TO' named entity 'LESS THAN' named entity 'REDUCE' named entity 'S CELL' named entity '20%' named entity 'GLYCOPROTEIN' named entity 'TRANSPORT' named entity 'PORTION' named entity 'THESE' named entity 'VIRUS ENTRY' named entity 'WILD-TYPE' named entity 'EVENTS' named entity 'CHANGES' named entity 'AMINO ACID' named entity 'SPIKE'

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