| pubmed-article:17134730 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17134730 | lifeskim:mentions | umls-concept:C1261468 | lld:lifeskim |
| pubmed-article:17134730 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:17134730 | lifeskim:mentions | umls-concept:C0598435 | lld:lifeskim |
| pubmed-article:17134730 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:17134730 | pubmed:dateCreated | 2007-4-2 | lld:pubmed |
| pubmed-article:17134730 | pubmed:abstractText | 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 (3)H-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. | lld:pubmed |
| pubmed-article:17134730 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17134730 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17134730 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17134730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17134730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17134730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17134730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17134730 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17134730 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17134730 | pubmed:issn | 0042-6822 | lld:pubmed |
| pubmed-article:17134730 | pubmed:author | pubmed-author:KousoulasK... | lld:pubmed |
| pubmed-article:17134730 | pubmed:author | pubmed-author:KnipeDavid... | lld:pubmed |
| pubmed-article:17134730 | pubmed:author | pubmed-author:ChouljenkoVla... | lld:pubmed |
| pubmed-article:17134730 | pubmed:author | pubmed-author:FarzanMichael... | lld:pubmed |
| pubmed-article:17134730 | pubmed:author | pubmed-author:PetitChad MCM | lld:pubmed |
| pubmed-article:17134730 | pubmed:author | pubmed-author:ColgroveRobin... | lld:pubmed |
| pubmed-article:17134730 | pubmed:author | pubmed-author:IyerArunA | lld:pubmed |
| pubmed-article:17134730 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17134730 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:17134730 | pubmed:volume | 360 | lld:pubmed |
| pubmed-article:17134730 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17134730 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17134730 | pubmed:pagination | 264-74 | lld:pubmed |
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| pubmed-article:17134730 | pubmed:meshHeading | pubmed-meshheading:17134730... | lld:pubmed |
| pubmed-article:17134730 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17134730 | pubmed:articleTitle | Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus spike glycoprotein is important for spike-mediated cell fusion. | lld:pubmed |
| pubmed-article:17134730 | pubmed:affiliation | Division of Biotechnology and Molecular Medicine (BIOMMED), USA. | lld:pubmed |
| pubmed-article:17134730 | pubmed:publicationType | Journal Article | lld:pubmed |
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