| pubmed-article:8189517 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8189517 | lifeskim:mentions | umls-concept:C0043396 | lld:lifeskim |
| pubmed-article:8189517 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:8189517 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:8189517 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8189517 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:8189517 | lifeskim:mentions | umls-concept:C0681829 | lld:lifeskim |
| pubmed-article:8189517 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:8189517 | pubmed:dateCreated | 1994-6-20 | lld:pubmed |
| pubmed-article:8189517 | pubmed:abstractText | Several of the cleavages required to generate the mature nonstructural proteins from the flaviviral polyprotein are known to be mediated by a complex consisting of NS2B and a serine proteinase domain located in the N-terminal one-third of NS3. These cleavages typically occur after two basic residues followed by a short side chain residue. Cleavage at a similar dibasic site in the structural region is believed to produce the C terminus of the virion capsid protein. To study this cleavage, we developed a cell-free trans cleavage assay for yellow fever virus (YF)-specific proteolytic activity by using a substrate spanning the C protein dibasic site. Cleavage at the predicted site was observed when the substrate was incubated with detergent-solubilized lysates from YF-infected BHK cells. NS2B and the NS3 proteinase domain were the only YF-specific proteins required for this cleavage. Cell fractionation studies demonstrated that the YF-specific proteolytic activity was membrane associated and that activity could be detected only after detergent solubilization. Previous cell-free studies led to a hypothesis that processing in the C-prM region involves (i) translation of C followed by translocation and core glycosylation of prM by using an internal signal sequence, (ii) signalase cleavage to produce a membrane-anchored form of the C protein (anchC) and the N terminus of prM, and (iii) NS2B-3-mediated cleavage at the anchC dibasic site to produce the C terminus of the virion C protein. However, the results of in vivo transient-expression studies do not support this temporal cleavage order. Rather, expression of a YF polyprotein extending from C through the N-terminal one-third of NS3 revealed that C-prM processing, but not translocation, was dependent on an active NS2B-3 proteinase. This suggests that signalase-mediated cleavage in the lumen of the endoplasmic reticulum may be dependent on prior cleavage at the anchC dibasic site. Possible pathways for processing in the C-prM region are outlined and discussed. | lld:pubmed |
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| pubmed-article:8189517 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8189517 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8189517 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8189517 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8189517 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8189517 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:8189517 | pubmed:author | pubmed-author:RichC RCR | lld:pubmed |
| pubmed-article:8189517 | pubmed:author | pubmed-author:McCourtD WDW | lld:pubmed |
| pubmed-article:8189517 | pubmed:author | pubmed-author:NestorowiczAA | lld:pubmed |
| pubmed-article:8189517 | pubmed:author | pubmed-author:AmbergS MSM | lld:pubmed |
| pubmed-article:8189517 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8189517 | pubmed:volume | 68 | lld:pubmed |
| pubmed-article:8189517 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8189517 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8189517 | pubmed:pagination | 3794-802 | lld:pubmed |
| pubmed-article:8189517 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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