| pubmed-article:15564482 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15564482 | lifeskim:mentions | umls-concept:C0017890 | lld:lifeskim |
| pubmed-article:15564482 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:15564482 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:15564482 | lifeskim:mentions | umls-concept:C0332466 | lld:lifeskim |
| pubmed-article:15564482 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:15564482 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15564482 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:15564482 | lifeskim:mentions | umls-concept:C0302891 | lld:lifeskim |
| pubmed-article:15564482 | lifeskim:mentions | umls-concept:C0030466 | lld:lifeskim |
| pubmed-article:15564482 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:15564482 | pubmed:dateCreated | 2004-11-26 | lld:pubmed |
| pubmed-article:15564482 | pubmed:abstractText | Hydrophobic fusion peptides (FPs) are the most highly conserved regions of class I viral fusion-mediating glycoproteins (vFGPs). FPs often contain conserved glycine residues thought to be critical for forming structures that destabilize target membranes. Unexpectedly, a mutation of glycine residues in the FP of the fusion (F) protein from the paramyxovirus simian parainfluenza virus 5 (SV5) resulted in mutant F proteins with hyperactive fusion phenotypes (C. M. Horvath and R. A. Lamb, J. Virol. 66:2443-2455, 1992). Here, we constructed G3A and G7A mutations into the F proteins of SV5 (W3A and WR isolates), Newcastle disease virus (NDV), and human parainfluenza virus type 3 (HPIV3). All of the mutant F proteins, except NDV G7A, caused increased cell-cell fusion despite having slight to moderate reductions in cell surface expression compared to those of wild-type F proteins. The G3A and G7A mutations cause SV5 WR F, but not NDV F or HPIV3 F, to be triggered to cause fusion in the absence of coexpression of its homotypic receptor-binding protein hemagglutinin-neuraminidase (HN), suggesting that NDV and HPIV3 F have stricter requirements for homotypic HN for fusion activation. Dye transfer assays show that the G3A and G7A mutations decrease the energy required to activate F at a step in the fusion cascade preceding prehairpin intermediate formation and hemifusion. Conserved glycine residues in the FP of paramyxovirus F appear to have a primary role in regulating the activation of the metastable native form of F. Glycine residues in the FPs of other class I vFGPs may also regulate fusion activation. | lld:pubmed |
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| pubmed-article:15564482 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15564482 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15564482 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15564482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15564482 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15564482 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:15564482 | pubmed:issn | 0022-538X | lld:pubmed |
