pubmed-article:20861246 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20861246 | lifeskim:mentions | umls-concept:C0206679 | lld:lifeskim |
pubmed-article:20861246 | lifeskim:mentions | umls-concept:C0021311 | lld:lifeskim |
pubmed-article:20861246 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
pubmed-article:20861246 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
pubmed-article:20861246 | lifeskim:mentions | umls-concept:C1704686 | lld:lifeskim |
pubmed-article:20861246 | lifeskim:mentions | umls-concept:C0205173 | lld:lifeskim |
pubmed-article:20861246 | pubmed:issue | 23 | lld:pubmed |
pubmed-article:20861246 | pubmed:dateCreated | 2010-11-4 | lld:pubmed |
pubmed-article:20861246 | pubmed:abstractText | Herpes simplex virus (HSV) entry into cells is triggered by the binding of envelope glycoprotein D (gD) to a specific receptor, such as nectin-1 or herpesvirus entry mediator (HVEM), resulting in activation of the fusion effectors gB and gH and virus penetration. Here we report the identification of a hyperactive gB allele, D285N/A549T, selected by repeat passage of a gD mutant virus defective for nectin-1 binding through cells that express a gD-binding-impaired mutant nectin-1. The gB allele in a wild-type virus background enabled the use of other nectins as virus entry receptors. In addition, combination of the mutant allele with an epidermal growth factor receptor (EGFR)-retargeted gD gene yielded dramatically increased EGFR-specific virus entry compared to retargeted virus carrying wild-type gB. Entry of the gB mutant virus into nectin-1-bearing cells was markedly accelerated compared to that of wild-type virus, suggesting that the gB mutations affect a rate-limiting step in entry. Our observations indicate that ineffective gD activation can be complemented by hypersensitization of a downstream component of the entry cascade to gD signaling. | lld:pubmed |
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pubmed-article:20861246 | pubmed:language | eng | lld:pubmed |
pubmed-article:20861246 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20861246 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20861246 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:20861246 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20861246 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20861246 | pubmed:month | Dec | lld:pubmed |
pubmed-article:20861246 | pubmed:issn | 1098-5514 | lld:pubmed |
pubmed-article:20861246 | pubmed:author | pubmed-author:GloriosoJosep... | lld:pubmed |
pubmed-article:20861246 | pubmed:author | pubmed-author:GrandiPaolaP | lld:pubmed |
pubmed-article:20861246 | pubmed:author | pubmed-author:GoinsWilliam... | lld:pubmed |
pubmed-article:20861246 | pubmed:author | pubmed-author:KumagaiIzumiI | lld:pubmed |
pubmed-article:20861246 | pubmed:author | pubmed-author:UchidaHiroaki... | lld:pubmed |
pubmed-article:20861246 | pubmed:author | pubmed-author:CohenJustus... | lld:pubmed |
pubmed-article:20861246 | pubmed:author | pubmed-author:ChanJanetJ | lld:pubmed |
pubmed-article:20861246 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20861246 | pubmed:volume | 84 | lld:pubmed |
pubmed-article:20861246 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20861246 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20861246 | pubmed:pagination | 12200-9 | lld:pubmed |
pubmed-article:20861246 | pubmed:dateRevised | 2011-7-28 | lld:pubmed |
pubmed-article:20861246 | pubmed:meshHeading | pubmed-meshheading:20861246... | lld:pubmed |
pubmed-article:20861246 | pubmed:meshHeading | pubmed-meshheading:20861246... | lld:pubmed |
pubmed-article:20861246 | pubmed:meshHeading | pubmed-meshheading:20861246... | lld:pubmed |
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