| pubmed-article:17959681 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17959681 | lifeskim:mentions | umls-concept:C0042760 | lld:lifeskim |
| pubmed-article:17959681 | lifeskim:mentions | umls-concept:C0206679 | lld:lifeskim |
| pubmed-article:17959681 | lifeskim:mentions | umls-concept:C0206355 | lld:lifeskim |
| pubmed-article:17959681 | lifeskim:mentions | umls-concept:C0243126 | lld:lifeskim |
| pubmed-article:17959681 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:17959681 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:17959681 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:17959681 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:17959681 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:17959681 | pubmed:dateCreated | 2007-12-11 | lld:pubmed |
| pubmed-article:17959681 | pubmed:abstractText | Early in infection, herpes simplex virus type 1 (HSV-1) immediate-early (IE) proteins ICP0 and ICP4 localize to the nucleus, where they stimulate viral transcription. Later in infection, ICP0 and to a lesser extent ICP4 accumulate in the cytoplasm, but their biological role there is unknown. Previously, it was shown that the cytoplasmic localization of ICP0/4 requires the multifunctional IE protein ICP27, which is itself an activator of viral gene expression. Here, we identify a viral ICP27 mutant, d3-4, which is unable to efficiently localize ICP0 and ICP4 to the cytoplasm but which otherwise resembles wild-type HSV-1 in its growth and viral gene expression phenotypes. These results genetically separate the function of ICP27 that affects ICP0/4 localization from its other functions, which affect viral growth and gene expression. As both ICP0 and ICP4 are known to be minor virion components, we used d3-4 to test the hypothesis that the cytoplasmic localization of these proteins is required for their incorporation into viral particles. Consistent with this conjecture, d3-4 virions were found to lack ICP0 in their tegument and to have greatly reduced levels of ICP4. Thus, the cytoplasmic localization of ICP0 and ICP4 appears to be a prerequisite for the assembly of these important transcriptional regulatory proteins into viral particles. Furthermore, our results show that ICP27 plays a previously unrecognized role in determining the composition of HSV-1 virions. | lld:pubmed |
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| pubmed-article:17959681 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17959681 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17959681 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17959681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17959681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17959681 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17959681 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:17959681 | pubmed:issn | 1098-5514 | lld:pubmed |
| pubmed-article:17959681 | pubmed:author | pubmed-author:RiceStephen... | lld:pubmed |
| pubmed-article:17959681 | pubmed:author | pubmed-author:SedlackovaLen... | lld:pubmed |
| pubmed-article:17959681 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17959681 | pubmed:volume | 82 | lld:pubmed |
| pubmed-article:17959681 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17959681 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17959681 | pubmed:pagination | 268-77 | lld:pubmed |
