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• W2025200316 endingPage "274" @default.
• W2025200316 startingPage "264" @default.
• W2025200316 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." @default.
• W2025200316 created "2016-06-24" @default.
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• W2025200316 creator A5042670469 @default.
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• W2025200316 date "2007-04-01" @default.
• W2025200316 modified "2023-10-11" @default.
• W2025200316 title "Palmitoylation of the cysteine-rich endodomain of the SARS–coronavirus spike glycoprotein is important for spike-mediated cell fusion" @default.
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• W2025200316 doi "https://doi.org/10.1016/j.virol.2006.10.034" @default.
• W2025200316 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7103323" @default.
• W2025200316 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17134730" @default.
• W2025200316 hasPublicationYear "2007" @default.
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