About: Genetic analysis of the SARS-coronavirus spike glycoprotein functional domains involved in cell-surface expression and cell-to-cell fusion

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About: Genetic analysis of the SARS-coronavirus spike glycoprotein functional domains involved in cell-surface expression and cell-to-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	Genetic analysis of the SARS-coronavirus spike glycoprotein functional domains involved in cell-surface expression and cell-to-cell fusion
Creator	Farzan, Michael Colgrove, Robin Knipe, David Chouljenko, Vladimir Kousoulas, K Melancon, Jeffrey Petit, Chad
Source	Elsevier; Medline; PMC
abstract	Abstract The SARS-coronavirus (SARS-CoV) is the etiological agent of 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. To delineate functional domains of the SARS-CoV S glycoprotein, single point mutations, cluster-to-lysine and cluster-to-alanine mutations, as well as carboxyl-terminal truncations were investigated in transient expression experiments. Mutagenesis of either the coiled-coil domain of the S glycoprotein amino terminal heptad repeat, the predicted fusion peptide, or an adjacent but distinct region, severely compromised S-mediated cell-to-cell fusion, while intracellular transport and cell-surface expression were not adversely affected. Surprisingly, a carboxyl-terminal truncation of 17 amino acids substantially increased S glycoprotein-mediated cell-to-cell fusion suggesting that the terminal 17 amino acids regulated the S fusogenic properties. In contrast, truncation of 26 or 39 amino acids eliminating either one or both of the two endodomain cysteine-rich motifs, respectively, inhibited cell fusion in comparison to the wild-type S. The 17 and 26 amino-acid deletions did not adversely affect S cell-surface expression, while the 39 amino-acid truncation inhibited S cell-surface expression suggesting that the membrane proximal cysteine-rich motif plays an essential role in S cell-surface expression. Mutagenesis of the acidic amino-acid cluster in the carboxyl terminus of the S glycoprotein as well as modification of a predicted phosphorylation site within the acidic cluster revealed that this amino-acid motif may play a functional role in the retention of S at cell surfaces. This genetic analysis reveals that the SARS-CoV S glycoprotein contains extracellular domains that regulate cell fusion as well as distinct endodomains that function in intracellular transport, cell-surface expression, and cell fusion.
has issue date	2005-10-25(xsd:dateTime)
bibo:doi	10.1016/j.virol.2005.06.046
bibo:pmid	16099010
has license	els-covid
sha1sum (hex)	416fe0579e576fd60909ac3cf3e9a0f5d751facf
schema:url	https://doi.org/10.1016/j.virol.2005.06.046
resource representing a document's title	Genetic analysis of the SARS-coronavirus spike glycoprotein functional domains involved in cell-surface expression and cell-to-cell fusion
has PubMed Central identifier	PMC7111838
has PubMed identifier	16099010
schema:publication	Virology
resource representing a document's body	covid:416fe0579e576fd60909ac3cf3e9a0f5d751facf#body_text
is schema:about of	named entity 'acidic' named entity 'glycoprotein' named entity 'expression' named entity 'SARS-CoV' named entity 'amino-acid' named entity 'PROXIMAL' named entity 'DELINEATE' named entity 'CONTAINS' named entity 'ROLE' named entity 'INTRACELLULAR TRANSPORT' named entity 'PREDICTED' named entity 'CLUSTER' named entity 'MUTAGENESIS' named entity 'SINGLE' named entity 'PLAYS' named entity 'TRANSIENT EXPRESSION' named entity 'AGENT' named entity 'FUNCTION' named entity 'MOTIFS' named entity 'VIRUS' named entity 'TERMINAL' named entity 'MODIFICATION' named entity 'ALANINE' named entity 'CONTRAST' named entity 'ESSENTIAL' named entity 'FUNCTIONAL ROLE' named entity 'CELL FUSION' named entity 'FUSION PEPTIDE' named entity 'BUT' named entity 'CELL FUSION' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME' named entity 'DISTINCT' named entity 'SEVERELY' named entity 'EXTRACELLULAR' named entity '2C CELL' named entity 'INDUCED' named entity 'CORONAVIRUS' named entity 'INVOLVED' named entity 'AFFECT' named entity 'COILED-COIL DOMAIN' named entity 'INVESTIGATED' named entity 'SURFACE' named entity 'GENETIC ANALYSIS' named entity 'SARS' named entity 'MEMBRANE' named entity 'GENETIC ANALYSIS' named entity 'TRUNCATION' named entity 'AMINO-ACID' named entity 'RETENTION' named entity 'AFFECTED' named entity 'FUNCTIONAL' named entity 'IN S' named entity 'VIRUS ENTRY' named entity 'S CELL' named entity 'REGION' named entity 'CORONAVIRUS' named entity 'CYSTEINE' named entity 'DID' named entity 'CELL' named entity 'EXPERIMENTS' named entity 'MEDIATES' named entity 'INHIBITED' named entity 'AMINO TERMINAL' named entity 'AMINO ACIDS' named entity 'SURFACE' named entity 'LYSINE' named entity 'EXPRESSION' named entity 'CELL' named entity 'FUNCTIONAL' named entity 'SARS-COV' named entity 'MOTIF' named entity 'REPEAT' named entity 'REGULATE' named entity 'EVENTS' named entity 'SPIKE'

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