Source:http://linkedlifedata.com/resource/pubmed/id/17134730
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
2007-4-2
|
| 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/spike glycoprotein, coronavirus
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0042-6822
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
10
|
| pubmed:volume |
360
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
264-74
|
| pubmed:meshHeading |
pubmed-meshheading:17134730-Amino Acid Sequence,
pubmed-meshheading:17134730-Animals,
pubmed-meshheading:17134730-Cell Fusion,
pubmed-meshheading:17134730-Cell Membrane,
pubmed-meshheading:17134730-Cercopithecus aethiops,
pubmed-meshheading:17134730-Cysteine,
pubmed-meshheading:17134730-Immunohistochemistry,
pubmed-meshheading:17134730-Isotope Labeling,
pubmed-meshheading:17134730-Membrane Fusion,
pubmed-meshheading:17134730-Membrane Glycoproteins,
pubmed-meshheading:17134730-Molecular Sequence Data,
pubmed-meshheading:17134730-Mutagenesis, Site-Directed,
pubmed-meshheading:17134730-Palmitic Acid,
pubmed-meshheading:17134730-Protein Processing, Post-Translational,
pubmed-meshheading:17134730-SARS Virus,
pubmed-meshheading:17134730-Tritium,
pubmed-meshheading:17134730-Vero Cells,
pubmed-meshheading:17134730-Viral Envelope Proteins
|
| pubmed:year |
2007
|
| pubmed:articleTitle |
Palmitoylation of the cysteine-rich endodomain of the SARS-coronavirus spike glycoprotein is important for spike-mediated cell fusion.
|
| pubmed:affiliation |
Division of Biotechnology and Molecular Medicine (BIOMMED), USA.
|
| pubmed:publicationType |
Journal Article
|