| pubmed-article:19710150 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19710150 | lifeskim:mentions | umls-concept:C0318798 | lld:lifeskim |
| pubmed-article:19710150 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:19710150 | lifeskim:mentions | umls-concept:C0332466 | lld:lifeskim |
| pubmed-article:19710150 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:19710150 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:19710150 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:19710150 | pubmed:dateCreated | 2009-10-9 | lld:pubmed |
| pubmed-article:19710150 | pubmed:abstractText | For paramyxoviruses, entry requires a receptor-binding protein (hemagglutinin-neuraminidase [HN], H, or G) and a fusion protein (F). Like other class I viral fusion proteins, F is expressed as a prefusion metastable protein that undergoes a refolding event to induce fusion. HN binding to its receptor triggers F refolding by an unknown mechanism. HN may serve as a clamp that stabilizes F in its prefusion state until HN binds the target cell (the "clamp model"). Alternatively, HN itself may undergo a conformational change after receptor binding that destabilizes F and causes F to trigger (the "provocateur model"). To examine F-HN interactions by bimolecular fluorescence complementation (BiFC), the cytoplasmic tails of parainfluenza virus 5 (PIV5) F and HN were fused to complementary fragments of yellow fluorescent protein (YFP). Coexpression of the BiFC constructs resulted in fluorescence; however, coexpression with unrelated BiFC constructs also produced fluorescence. The affinity of the two halves of YFP presumably superseded the F-HN interaction. Unexpectedly, coexpression of the BiFC F and HN constructs greatly enhanced fusion in multiple cell types. We hypothesize that the increase in fusion occurs because the BiFC tags bring F and HN together more frequently than occurs in a wild-type (wt) scenario. This implies that normally much of wt F is not associated with wt HN, in conflict with the clamp model for activation. Correspondingly, we show that wt PIV5 fusion occurs in an HN concentration-dependent manner. Also inconsistent with the clamp model are the findings that BiFC F does not adopt a postfusion conformation when expressed in the absence of HN and that HN coexpression does not provide resistance to the heat-induced triggering of F. In support of a provocateur model of F activation, we demonstrate by analysis of the morphology of soluble F trimers that the hyperfusogenic mutation S443P has a destabilizing effect on F. | lld:pubmed |
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| pubmed-article:19710150 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19710150 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19710150 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19710150 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19710150 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:19710150 | pubmed:issn | 1098-5514 | lld:pubmed |
| pubmed-article:19710150 | pubmed:author | pubmed-author:LambRobert... | lld:pubmed |
| pubmed-article:19710150 | pubmed:author | pubmed-author:JardetzkyTheo... | lld:pubmed |
| pubmed-article:19710150 | pubmed:author | pubmed-author:LeserGeorge... | lld:pubmed |
| pubmed-article:19710150 | pubmed:author | pubmed-author:ConnollySarah... | lld:pubmed |
